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| <StructureSection load='1vrn' size='340' side='right'caption='[[1vrn]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1vrn' size='340' side='right'caption='[[1vrn]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1vrn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1txw 1txw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VRN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vrn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1txw 1txw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VRN FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ7:UBIQUINONE-7'>UQ7</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ7:UBIQUINONE-7'>UQ7</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r2c|1r2c]]</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=1vrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrn OCA], [https://pdbe.org/1vrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vrn RCSB], [https://www.ebi.ac.uk/pdbsum/1vrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrn 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=1vrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrn OCA], [http://pdbe.org/1vrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vrn RCSB], [http://www.ebi.ac.uk/pdbsum/1vrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vrn ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/RCEM_RHOVI RCEM_RHOVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/CYCR_RHOVI CYCR_RHOVI]] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. [[http://www.uniprot.org/uniprot/RCEL_RHOVI RCEL_RHOVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEH_RHOVI RCEH_RHOVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | + | [https://www.uniprot.org/uniprot/CYCR_BLAVI CYCR_BLAVI] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.<ref>PMID:10736158</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| [[Category: Blastochloris viridis]] | | [[Category: Blastochloris viridis]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Baxter, R H.G]] | + | [[Category: Baxter RHG]] |
- | [[Category: Norris, J R]] | + | [[Category: Norris JR]] |
- | [[Category: Seagle, B L]] | + | [[Category: Seagle B-L]] |
- | [[Category: Integral membrane protein]]
| + | |
- | [[Category: Photosynthesis]]
| + | |
- | [[Category: Ubiquinone]]
| + | |
| Structural highlights
1vrn is a 4 chain structure with sequence from Blastochloris viridis. This structure supersedes the now removed PDB entry 1txw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 2.2Å |
Ligands: | , , , , , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CYCR_BLAVI The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[1]
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 PubMed
The structure of the Blastochloris viridis photosynthetic reaction center has been determined at 100 K by flash-freezing crystals. A data set to 2.2 A resolution provides a well determined model of the wild-type protein. Of particular interest are the position, occupancy and heterogeneity of the Q(B)-binding site. Data were also collected from a crystal frozen immediately after illumination. The data support predominant binding of Q(B) in the proximal position in both the neutral and charge-separated states.
Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark.,Baxter RH, Seagle BL, Ponomarenko N, Norris JR Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):605-12. Epub 2005, Apr 20. PMID:15858271[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen IP, Mathis P, Koepke J, Michel H. Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis. Biochemistry. 2000 Apr 4;39(13):3592-602. PMID:10736158
- ↑ Baxter RH, Seagle BL, Ponomarenko N, Norris JR. Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark. Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):605-12. Epub 2005, Apr 20. PMID:15858271 doi:10.1107/S0907444905005809
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