4ub6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
{{Large structure}}
 
==Native structure of photosystem II (dataset-1) by a femtosecond X-ray laser==
==Native structure of photosystem II (dataset-1) by a femtosecond X-ray laser==
<StructureSection load='4ub6' size='340' side='right' caption='[[4ub6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='4ub6' size='340' side='right'caption='[[4ub6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ub6]] is a 39 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_vulcanus Thermosynechococcus vulcanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UB6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ub6]] is a 39 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_vulcanus Thermosynechococcus vulcanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UB6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HTG:HEPTYL+1-THIOHEXOPYRANOSIDE'>HTG</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OEX:CA-MN4-O5+CLUSTER'>OEX</scene>, <scene name='pdbligand=PHO:PHEOPHYTIN+A'>PHO</scene>, <scene name='pdbligand=PL9:2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE'>PL9</scene>, <scene name='pdbligand=SQD:1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL'>SQD</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HTG:HEPTYL+1-THIOHEXOPYRANOSIDE'>HTG</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OEX:CA-MN4-O5+CLUSTER'>OEX</scene>, <scene name='pdbligand=PHO:PHEOPHYTIN+A'>PHO</scene>, <scene name='pdbligand=PL9:2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE'>PL9</scene>, <scene name='pdbligand=SQD:1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL'>SQD</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ub8|4ub8]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ub8|4ub8]]</td></tr>
Line 10: Line 10:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ub6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ub6 OCA], [http://pdbe.org/4ub6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ub6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ub6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ub6 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ub6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ub6 OCA], [http://pdbe.org/4ub6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ub6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ub6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ub6 ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PSBL_THEVL PSBL_THEVL]] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01317] [[http://www.uniprot.org/uniprot/YCF12_THEVL YCF12_THEVL]] A core subunit of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBB_THEVL PSBB_THEVL]] This protein binds multiple antenna chlorophylls and is part of the core of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBX_THEVL PSBX_THEVL]] Involved in the binding and/or turnover of quinones at the Q(B) site of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01386] [[http://www.uniprot.org/uniprot/CY550_THEVL CY550_THEVL]] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.<ref>PMID:1314738</ref> <ref>PMID:8382523</ref>  [[http://www.uniprot.org/uniprot/PSBO_THEVL PSBO_THEVL]] Part of the oxygen-evolving complex associated with photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBF_THEVL PSBF_THEVL]] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00643] [[http://www.uniprot.org/uniprot/PSBJ_THEVL PSBJ_THEVL]] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01305] [[http://www.uniprot.org/uniprot/PSBT_THEVL PSBT_THEVL]] Seems to play a role in the dimerization of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00808] [[http://www.uniprot.org/uniprot/PSBI_THEVL PSBI_THEVL]] A component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01316] [[http://www.uniprot.org/uniprot/PSBD_THEVL PSBD_THEVL]] D1 (PsbA) and D2 (PsbD) bind P680, the primary electron donor of photosystem II (PSII) as well as electron acceptors. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. D2 is needed for assembly of a stable PSII complex.[HAMAP-Rule:MF_01383] [[http://www.uniprot.org/uniprot/PSBZ_THEVL PSBZ_THEVL]] Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00644] [[http://www.uniprot.org/uniprot/PSBE_THEVL PSBE_THEVL]] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00642]  
[[http://www.uniprot.org/uniprot/PSBL_THEVL PSBL_THEVL]] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01317] [[http://www.uniprot.org/uniprot/YCF12_THEVL YCF12_THEVL]] A core subunit of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBB_THEVL PSBB_THEVL]] This protein binds multiple antenna chlorophylls and is part of the core of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBX_THEVL PSBX_THEVL]] Involved in the binding and/or turnover of quinones at the Q(B) site of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01386] [[http://www.uniprot.org/uniprot/CY550_THEVL CY550_THEVL]] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.<ref>PMID:1314738</ref> <ref>PMID:8382523</ref>  [[http://www.uniprot.org/uniprot/PSBO_THEVL PSBO_THEVL]] Part of the oxygen-evolving complex associated with photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [[http://www.uniprot.org/uniprot/PSBF_THEVL PSBF_THEVL]] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00643] [[http://www.uniprot.org/uniprot/PSBJ_THEVL PSBJ_THEVL]] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01305] [[http://www.uniprot.org/uniprot/PSBT_THEVL PSBT_THEVL]] Seems to play a role in the dimerization of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00808] [[http://www.uniprot.org/uniprot/PSBI_THEVL PSBI_THEVL]] A component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01316] [[http://www.uniprot.org/uniprot/PSBD_THEVL PSBD_THEVL]] D1 (PsbA) and D2 (PsbD) bind P680, the primary electron donor of photosystem II (PSII) as well as electron acceptors. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. D2 is needed for assembly of a stable PSII complex.[HAMAP-Rule:MF_01383] [[http://www.uniprot.org/uniprot/PSBZ_THEVL PSBZ_THEVL]] Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00644] [[http://www.uniprot.org/uniprot/PSBE_THEVL PSBE_THEVL]] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00642]  
Line 22: Line 21:
</div>
</div>
<div class="pdbe-citations 4ub6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4ub6" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Photosystem II|Photosystem II]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Photosystem II]]
[[Category: Photosystem II]]
[[Category: Thermosynechococcus vulcanus]]
[[Category: Thermosynechococcus vulcanus]]

Revision as of 13:48, 2 October 2019

Native structure of photosystem II (dataset-1) by a femtosecond X-ray laserNative structure of photosystem II (dataset-1) by a femtosecond X-ray laser

Structural highlights

4ub6 is a 39 chain structure with sequence from Thermosynechococcus vulcanus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , , , , , , , , , , , , , ,
NonStd Res:
Activity:Photosystem II, with EC number 1.10.3.9
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSBL_THEVL] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01317] [YCF12_THEVL] A core subunit of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [PSBB_THEVL] This protein binds multiple antenna chlorophylls and is part of the core of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [PSBX_THEVL] Involved in the binding and/or turnover of quinones at the Q(B) site of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01386] [CY550_THEVL] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[1] [2] [PSBO_THEVL] Part of the oxygen-evolving complex associated with photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. [PSBF_THEVL] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00643] [PSBJ_THEVL] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01305] [PSBT_THEVL] Seems to play a role in the dimerization of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00808] [PSBI_THEVL] A component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01316] [PSBD_THEVL] D1 (PsbA) and D2 (PsbD) bind P680, the primary electron donor of photosystem II (PSII) as well as electron acceptors. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. D2 is needed for assembly of a stable PSII complex.[HAMAP-Rule:MF_01383] [PSBZ_THEVL] Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00644] [PSBE_THEVL] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00642]

Publication Abstract from PubMed

Photosynthesis converts light energy into biologically useful chemical energy vital to life on Earth. The initial reaction of photosynthesis takes place in photosystem II (PSII), a 700-kilodalton homodimeric membrane protein complex that catalyses photo-oxidation of water into dioxygen through an S-state cycle of the oxygen evolving complex (OEC). The structure of PSII has been solved by X-ray diffraction (XRD) at 1.9 angstrom resolution, which revealed that the OEC is a Mn4CaO5-cluster coordinated by a well defined protein environment. However, extended X-ray absorption fine structure (EXAFS) studies showed that the manganese cations in the OEC are easily reduced by X-ray irradiation, and slight differences were found in the Mn-Mn distances determined by XRD, EXAFS and theoretical studies. Here we report a 'radiation-damage-free' structure of PSII from Thermosynechococcus vulcanus in the S1 state at a resolution of 1.95 angstroms using femtosecond X-ray pulses of the SPring-8 angstrom compact free-electron laser (SACLA) and hundreds of large, highly isomorphous PSII crystals. Compared with the structure from XRD, the OEC in the X-ray free electron laser structure has Mn-Mn distances that are shorter by 0.1-0.2 angstroms. The valences of each manganese atom were tentatively assigned as Mn1D(III), Mn2C(IV), Mn3B(IV) and Mn4A(III), based on the average Mn-ligand distances and analysis of the Jahn-Teller axis on Mn(III). One of the oxo-bridged oxygens, O5, has significantly longer distances to Mn than do the other oxo-oxygen atoms, suggesting that O5 is a hydroxide ion instead of a normal oxygen dianion and therefore may serve as one of the substrate oxygen atoms. These findings provide a structural basis for the mechanism of oxygen evolution, and we expect that this structure will provide a blueprint for the design of artificial catalysts for water oxidation.

Native structure of photosystem II at 1.95 A resolution viewed by femtosecond X-ray pulses.,Suga M, Akita F, Hirata K, Ueno G, Murakami H, Nakajima Y, Shimizu T, Yamashita K, Yamamoto M, Ago H, Shen JR Nature. 2015 Jan 1;517(7532):99-103. doi: 10.1038/nature13991. Epub 2014 Nov 26. PMID:25470056[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Shen JR, Ikeuchi M, Inoue Y. Stoichiometric association of extrinsic cytochrome c550 and 12 kDa protein with a highly purified oxygen-evolving photosystem II core complex from Synechococcus vulcanus. FEBS Lett. 1992 Apr 20;301(2):145-9. PMID:1314738
  2. Shen JR, Inoue Y. Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II. Biochemistry. 1993 Feb 23;32(7):1825-32. PMID:8382523
  3. Suga M, Akita F, Hirata K, Ueno G, Murakami H, Nakajima Y, Shimizu T, Yamashita K, Yamamoto M, Ago H, Shen JR. Native structure of photosystem II at 1.95 A resolution viewed by femtosecond X-ray pulses. Nature. 2015 Jan 1;517(7532):99-103. doi: 10.1038/nature13991. Epub 2014 Nov 26. PMID:25470056 doi:http://dx.doi.org/10.1038/nature13991

4ub6, resolution 1.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA