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New page: left|200px<br /><applet load="1aig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aig, resolution 2.6Å" /> '''PHOTOSYNTHETIC REACTI...
 
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[[Image:1aig.gif|left|200px]]<br /><applet load="1aig" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aig, resolution 2.6&Aring;" />
'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE'''<br />


==Overview==
==PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE==
High resolution x-ray diffraction data from crystals of the Rhodobacter, sphaeroides photosynthetic reaction center (RC) have been collected at, cryogenic temperature in the dark and under illumination, and the, structures were refined at 2.2 and 2.6 angstrom resolution, respectively., In the charge-separated D+QAQB- state (where D is the primary electron, donor (a bacteriochlorophyll dimer), and QA and QB are the primary and, secondary quinone acceptors, respectively), QB- is located approximately 5, angstroms from the QB position in the charge-neutral (DQAQB) state, and, has undergone a 180 degrees propeller twist around the isoprene chain. A, model based on the difference between the two structures is proposed to, explain the observed kinetics of electron transfer from QA-QB to QAQB- and, the relative binding affinities of the different ubiquinone species in the, QB pocket. In addition, several water channels (putative proton pathways), leading from the QB pocket to the surface of the RC were delineated, one, of which leads directly to the membrane surface.
<StructureSection load='1aig' size='340' side='right'caption='[[1aig]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aig]] is a 6 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=1AIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=1aig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aig OCA], [https://pdbe.org/1aig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aig RCSB], [https://www.ebi.ac.uk/pdbsum/1aig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aig ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RCEM_CERSP RCEM_CERSP] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1aig_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1aig ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
High resolution x-ray diffraction data from crystals of the Rhodobacter sphaeroides photosynthetic reaction center (RC) have been collected at cryogenic temperature in the dark and under illumination, and the structures were refined at 2.2 and 2.6 angstrom resolution, respectively. In the charge-separated D+QAQB- state (where D is the primary electron donor (a bacteriochlorophyll dimer), and QA and QB are the primary and secondary quinone acceptors, respectively), QB- is located approximately 5 angstroms from the QB position in the charge-neutral (DQAQB) state, and has undergone a 180 degrees propeller twist around the isoprene chain. A model based on the difference between the two structures is proposed to explain the observed kinetics of electron transfer from QA-QB to QAQB- and the relative binding affinities of the different ubiquinone species in the QB pocket. In addition, several water channels (putative proton pathways) leading from the QB pocket to the surface of the RC were delineated, one of which leads directly to the membrane surface.


==About this Structure==
Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer.,Stowell MH, McPhillips TM, Rees DC, Soltis SM, Abresch E, Feher G Science. 1997 May 2;276(5313):812-6. PMID:9115209<ref>PMID:9115209</ref>
1AIG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE2, BCL, BPH and U10 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AIG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer., Stowell MH, McPhillips TM, Rees DC, Soltis SM, Abresch E, Feher G, Science. 1997 May 2;276(5313):812-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9115209 9115209]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1aig" style="background-color:#fffaf0;"></div>
[[Category: Rhodobacter sphaeroides]]
== References ==
[[Category: Abresch, E.]]
<references/>
[[Category: Feher, G.]]
__TOC__
[[Category: Mcphillips, T.M.]]
</StructureSection>
[[Category: Rees, D.C.]]
[[Category: Cereibacter sphaeroides]]
[[Category: Soltis, S.M.]]
[[Category: Large Structures]]
[[Category: Stowell, M.H.B.]]
[[Category: Abresch E]]
[[Category: BCL]]
[[Category: Feher G]]
[[Category: BPH]]
[[Category: Mcphillips TM]]
[[Category: FE2]]
[[Category: Rees DC]]
[[Category: U10]]
[[Category: Soltis SM]]
[[Category: charge separated]]
[[Category: Stowell MHB]]
[[Category: integral membrane protein]]
[[Category: photosynthetic reaction center]]
 
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