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2rcr
From Proteopedia
(Difference between revisions)
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<StructureSection load='2rcr' size='340' side='right'caption='[[2rcr]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='2rcr' size='340' side='right'caption='[[2rcr]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2rcr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2rcr]] 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=2RCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCR 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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=UQ:COENZYME+Q10,+(2Z,6E,10Z,14E,18E,22E,26Z)-ISOMER'>UQ</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]] 3.1Å</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=UQ:COENZYME+Q10,+(2Z,6E,10Z,14E,18E,22E,26Z)-ISOMER'>UQ</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=2rcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcr OCA], [https://pdbe.org/2rcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcr RCSB], [https://www.ebi.ac.uk/pdbsum/2rcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcr 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=2rcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcr OCA], [https://pdbe.org/2rcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcr RCSB], [https://www.ebi.ac.uk/pdbsum/2rcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RCEH_CERSP RCEH_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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rcr ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rcr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides was determined at 3.1-A resolution by the molecular replacement method, using the Rhodopseudomonas viridis RC as the search structure. Atomic coordinates were refined with the difference Fourier method and restrained least-squares refinement techniques to a current R factor of 22%. The tertiary structure of the RC complex is stabilized by hydrophobic interactions between the L and M chains, by interactions of the pigments with each other and with the L and M chains, by residues from the L and M chains that coordinate to the Fe2+, by salt bridges that are formed between the L and M chains and the H chain, and possibly by electrostatic forces between the ends of helices. The conserved residues at the N-termini of the L and M chains were identified as recognition sites for the H chain. | ||
| - | |||
| - | Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.,Chang CH, el-Kabbani O, Tiede D, Norris J, Schiffer M Biochemistry. 1991 Jun 4;30(22):5352-60. PMID:2036404<ref>PMID:2036404</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2rcr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Cereibacter sphaeroides]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chang | + | [[Category: Chang C-H]] |
| - | [[Category: Norris | + | [[Category: Norris J]] |
| - | [[Category: Schiffer | + | [[Category: Schiffer M]] |
| - | + | ||
Current revision
STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES
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