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4v9g

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<StructureSection load='4v9g' size='340' side='right'caption='[[4v9g]], [[Resolution|resolution]] 7.78&Aring;' scene=''>
<StructureSection load='4v9g' size='340' side='right'caption='[[4v9g]], [[Resolution|resolution]] 7.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4v9g]] is a 64 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4jc9 4jc9] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4jcb 4jcb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V9G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4v9g]] is a 64 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4jc9 4jc9] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4jcb 4jcb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V9G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 7.78&#8491;</td></tr>
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<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=4v9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v9g OCA], [http://pdbe.org/4v9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v9g RCSB], [http://www.ebi.ac.uk/pdbsum/4v9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v9g ProSAT]</span></td></tr>
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<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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v9g OCA], [https://pdbe.org/4v9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v9g RCSB], [https://www.ebi.ac.uk/pdbsum/4v9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v9g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RCEM_RHOSH RCEM_RHOSH]] 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_RHOSH RCEH_RHOSH]] 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/LHB1_RHOS4 LHB1_RHOS4]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. [[http://www.uniprot.org/uniprot/PUFX_RHOS4 PUFX_RHOS4]] Associated with the reaction center - light-harvesting complex I. May play a critical role in facilitating the interaction between this complex and other components required for light-driven cyclic electron transfer. [[http://www.uniprot.org/uniprot/RCEL_RHOSH RCEL_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
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[https://www.uniprot.org/uniprot/LHA1_CERSP LHA1_CERSP]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Reaction center-light harvesting 1 (RC-LH1) complexes are the fundamental units of bacterial photosynthesis, which use solar energy to power the reduction of quinone to quinol prior to the formation of the proton gradient that drives ATP synthesis. The dimeric RC-LH1-PufX complex of Rhodobacter sphaeroides is composed of 64 polypeptides and 128 cofactors, including 56 LH1 bacteriochlorophyll a (BChl a) molecules that surround and donate energy to the two RCs. The 3D structure was determined to 8 A by X-ray crystallography, and a model was built with constraints provided by electron microscopy (EM), nuclear magnetic resonance (NMR), mass spectrometry (MS), and site-directed mutagenesis. Each half of the dimer complex consists of a RC surrounded by an array of 14 LH1 alphabeta subunits, with two BChls sandwiched between each alphabeta pair of transmembrane helices. The N- and C-terminal extrinsic domains of PufX promote dimerization by interacting with the corresponding domains of an LH1 beta polypeptide from the other half of the RC-LH1-PufX complex. Close contacts between PufX, an LH1 alphabeta subunit, and the cytoplasmic domain of the RC-H subunit prevent the LH1 complex from encircling the RC and create a channel connecting the RC QB site to an opening in the LH1 ring, allowing Q/QH2 exchange with the external quinone pool. We also identified a channel that connects the two halves of the dimer, potentially forming a long-range pathway for quinone migration along rows of RC-LH1-PufX complexes in the membrane. The structure of the RC-LH1-PufX complex explains the crucial role played by PufX in dimer formation, and it shows how quinone traffic traverses the LH1 complex as it shuttles between the RC and the cytochrome bc1 complex.
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Three-Dimensional Structure of the Rhodobacter sphaeroides RC-LH1-PufX Complex: Dimerization and Quinone Channels Promoted by PufX.,Qian P, Papiz MZ, Jackson PJ, Brindley AA, Ng IW, Olsen JD, Dickman MJ, Bullough PA, Hunter CN Biochemistry. 2013 Oct 16. PMID:24131108<ref>PMID:24131108</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4v9g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cereibacter sphaeroides]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Brindley AA]]
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[[Category: Brindley, A A]]
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[[Category: Bullough PA]]
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[[Category: Bullough, P A]]
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[[Category: Dickman MJ]]
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[[Category: Dickman, M J]]
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[[Category: Hunter CN]]
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[[Category: Hunter, C N]]
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[[Category: Jackson PJ]]
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[[Category: Jackson, P J]]
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[[Category: Ng IW]]
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[[Category: Ng, I W]]
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[[Category: Olsen JD]]
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[[Category: Olsen, J D]]
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[[Category: Papiz MZ]]
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[[Category: Papiz, M Z]]
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[[Category: Qian P]]
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[[Category: Qian, P]]
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[[Category: Antenna complex lh1]]
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[[Category: Chromophore]]
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[[Category: Membrane spherical vesicle]]
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[[Category: Photosynthesis]]
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[[Category: Photosynthetic chromophore]]
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[[Category: Photosynthetic complex]]
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[[Category: Photosynthetic light capture and electron transfer]]
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[[Category: Pufx]]
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[[Category: Quinol]]
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[[Category: Quinone]]
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[[Category: Reaction centre]]
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Current revision

RC-LH1-PufX dimer complex from Rhodobacter sphaeroides

PDB ID 4v9g

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