2wx5: Difference between revisions
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<StructureSection load='2wx5' size='340' side='right'caption='[[2wx5]], [[Resolution|resolution]] 2.63Å' scene=''> | <StructureSection load='2wx5' size='340' side='right'caption='[[2wx5]], [[Resolution|resolution]] 2.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wx5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2wx5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WX5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx5 OCA], [https://pdbe.org/2wx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2wx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx5 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx5 OCA], [https://pdbe.org/2wx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2wx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RCEH_CERS4 RCEH_CERS4] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cereibacter sphaeroides]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Crouch | [[Category: Crouch LI]] | ||
[[Category: Frolov | [[Category: Frolov D]] | ||
[[Category: Fyfe | [[Category: Fyfe PK]] | ||
[[Category: Hadfield AT]] | |||
[[Category: Hadfield | [[Category: Jones MR]] | ||
[[Category: Jones | [[Category: Marsh M]] | ||
[[Category: Marsh | [[Category: Robert B]] | ||
[[Category: Robert | [[Category: Van Grondelle R]] | ||
[[Category: | |||
Latest revision as of 13:18, 20 December 2023
Hexa-coordination of a bacteriochlorophyll cofactor in the Rhodobacter sphaeroides reaction centreHexa-coordination of a bacteriochlorophyll cofactor in the Rhodobacter sphaeroides reaction centre
Structural highlights
FunctionRCEH_CERS4 The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structural and functional consequences of changing the coordination state of one of the bacteriochlorophyll (BChl) cofactors in the purple bacterial reaction center have been explored. A combination of steady state spectroscopy and X-ray crystallography was used to demonstrate that mutagenesis of residue 181 of the L-polypeptide from Phe to Arg (FL181R) causes the BChl at the accessory (BB) position on the so-called inactive cofactor branch to become hexa-coordinated, with no significant changes to the structure of the surrounding protein. This change was accompanied by the appearance of a distinctive absorbance band at 631 nm in the room temperature absorbance spectrum. The ligand donor was not the Arg side chain but rather an intervening water molecule, and contrary to expectations the Mg of BB did not adopt a more in-plane geometry in response to hexa-coordination. The mutation caused a disturbance to the detailed conformation of the BChl macrocycle that manifested in a number of subtle changes to the resonance Raman spectrum. Hexa-coordination of BB produced a small increase in the lifetime of the excited electronic state of the primary donor bacteriochlorophylls (P*), indicating some disturbance to light-driven energy and/or electron transfer events on the time-scale of a few picoseconds after light excitation. The BB bacteriochlorophyll returned to a penta-coordinated state in a double mutant where the FL181R mutation was combined with removal of the native axial ligand through mutation of His M182 to Leu. Experimental evidence for hexa-coordinated bacteriochlorophylls in the literature on antenna proteins is considered, and possible reasons why hexa-coordinated bacteriochlorophylls and chlorophylls appear to be avoided in photosynthetic proteins are discussed. Structural and spectroscopic consequences of hexa-coordination of a bacteriochlorophyll cofactor in the Rhodobacter sphaeroides reaction center.,Frolov D, Marsh M, Crouch LI, Fyfe PK, Robert B, van Grondelle R, Hadfield A, Jones MR Biochemistry. 2010 Jan 29. PMID:20112981[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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