1aig: Difference between revisions

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[[Image:1aig.gif|left|200px]]


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==PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE==
The line below this paragraph, containing "STRUCTURE_1aig", creates the "Structure Box" on the page.
<StructureSection load='1aig' size='340' side='right'caption='[[1aig]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1aig| PDB=1aig |  SCENE= }}
<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>
'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE'''
== 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 ==
==Overview==
[[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.
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 [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.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://www.ncbi.nlm.nih.gov/pubmed/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: Charge separated]]
[[Category: Feher G]]
[[Category: Integral membrane protein]]
[[Category: Mcphillips TM]]
[[Category: Photosynthetic reaction center]]
[[Category: Rees DC]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:18:33 2008''
[[Category: Soltis SM]]
[[Category: Stowell MHB]]

Latest revision as of 05:22, 13 August 2026

PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE

1aig, resolution 2.60Å

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