2gmr: Difference between revisions
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<StructureSection load='2gmr' size='340' side='right'caption='[[2gmr]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2gmr' size='340' side='right'caption='[[2gmr]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gmr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2gmr]] 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=2GMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GMR 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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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]] 2.5Å</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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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=2gmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmr OCA], [https://pdbe.org/2gmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gmr RCSB], [https://www.ebi.ac.uk/pdbsum/2gmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gmr 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=2gmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmr OCA], [https://pdbe.org/2gmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gmr RCSB], [https://www.ebi.ac.uk/pdbsum/2gmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gmr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RCEL_CERSP RCEL_CERSP] 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: Cereibacter sphaeroides]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gerwert | [[Category: Gerwert K]] | ||
[[Category: Hermes | [[Category: Hermes S]] | ||
[[Category: Hofmann | [[Category: Hofmann E]] | ||
[[Category: Stachnik | [[Category: Stachnik JM]] | ||
Latest revision as of 12:44, 30 August 2023
Photosynthetic reaction center mutant from Rhodobacter sphaeroides with Asp L210 replaced with AsnPhotosynthetic reaction center mutant from Rhodobacter sphaeroides with Asp L210 replaced with Asn
Structural highlights
FunctionRCEL_CERSP 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 reaction center (RC) of Rhodobacter sphaeroides uses light energy to reduce and protonate a quinone molecule, QB (the secondary quinone electron acceptor), to form quinol, QBH2. Asp210 in the L-subunit has been shown to be a catalytic residue in this process. Mutation of Asp210 to Asn leads to a deceleration of reoxidation of QA- in the QA-QB --> QAQB- transition. Here we determined the structure of the Asp210 to Asn mutant to 2.5 A and show that there are no major structural differences as compared to the wild-type protein. We found QB in the distal position and a chain of water molecules between Asn210 and QB. Using time-resolved Fourier transform infrared (trFTIR) spectroscopy, we characterized the molecular reaction mechanism of this mutant. We found that QB- formation precedes QA- oxidation even more pronounced than in the wild-type reaction center. Continuum absorbance changes indicate deprotonation of a protonated water cluster, most likely of the water chain between Asn210 and QB. A detailed analysis of wild-type structures revealed a highly conserved water chain between Asp210 or Glu210 and QB in Rb. sphaeroides and Rhodopseudomonas viridis, respectively. Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules.,Hermes S, Stachnik JM, Onidas D, Remy A, Hofmann E, Gerwert K Biochemistry. 2006 Nov 21;45(46):13741-9. PMID:17105193[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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