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1r2c

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PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)

Structural highlights

1r2c is a 4 chain structure with sequence from Blastochloris viridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.86Å
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

Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).

Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.,Baxter RH, Ponomarenko N, Srajer V, Pahl R, Moffat K, Norris JR Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5982-7. Epub 2004 Apr 8. PMID:15073325^[2]

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

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, Ponomarenko N, Srajer V, Pahl R, Moffat K, Norris JR. Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5982-7. Epub 2004 Apr 8. PMID:15073325 doi:10.1073/pnas.0306840101

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r2c"

@@ Line 3: / Line 3: @@
 <StructureSection load='1r2c' size='340' side='right'caption='[[1r2c]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1r2c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R2C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1r2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R2C 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=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</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]] 2.86&#8491;</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></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=1r2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2c OCA], [http://pdbe.org/1r2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r2c RCSB], [http://www.ebi.ac.uk/pdbsum/1r2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r2c 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=1r2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2c OCA], [https://pdbe.org/1r2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r2c RCSB], [https://www.ebi.ac.uk/pdbsum/1r2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r2c ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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. [[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/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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 38: @@
 [[Category: Blastochloris viridis]]
 [[Category: Large Structures]]
-[[Category: Baxter, R H]]
+[[Category: Baxter RH]]
-[[Category: Moffat, K]]
+[[Category: Moffat K]]
-[[Category: Norris, J R]]
+[[Category: Norris JR]]
-[[Category: Pahl, R]]
+[[Category: Pahl R]]
-[[Category: Ponomarenko, N]]
+[[Category: Ponomarenko N]]
-[[Category: Srajer, V]]
+[[Category: Srajer V]]
-[[Category: Photosynthesis]]
-[[Category: Photosynthetic reaction center]]

1r2c

From Proteopedia

Current revision

PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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