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==X-RAY HIGH RESOLUTION STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTER FROM RB. SPHAEROIDES AT PH 9 IN THE CHARGE-SEPARATED STATE, 2ND DATASET==
 
<StructureSection load='2ux4' size='340' side='right' caption='[[2ux4]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
==X-ray high resolution structure of the photosynthetic reaction center from Rb. sphaeroides at pH 9 in the charge-separated state, 2nd dataset==
<StructureSection load='2ux4' size='340' side='right'caption='[[2ux4]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ux4]] is a 3 chain structure with sequence 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=2UX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UX4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ux4]] 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=2UX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UX4 FirstGlance]. <br>
</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=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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]] 2.51&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aig|1aig]], [[1aij|1aij]], [[1ds8|1ds8]], [[1dv3|1dv3]], [[1dv6|1dv6]], [[1e14|1e14]], [[1e6d|1e6d]], [[1f6n|1f6n]], [[1fnp|1fnp]], [[1fnq|1fnq]], [[1jgw|1jgw]], [[1jgx|1jgx]], [[1jgy|1jgy]], [[1jgz|1jgz]], [[1jh0|1jh0]], [[1k6l|1k6l]], [[1k6n|1k6n]], [[1kby|1kby]], [[1l9b|1l9b]], [[1l9j|1l9j]], [[1m3x|1m3x]], [[1mps|1mps]], [[1ogv|1ogv]], [[1pcr|1pcr]], [[1pss|1pss]], [[1pst|1pst]], [[1qov|1qov]], [[1rg5|1rg5]], [[1rgn|1rgn]], [[1rqk|1rqk]], [[1rvj|1rvj]], [[1ry5|1ry5]], [[1rzh|1rzh]], [[1rzz|1rzz]], [[1s00|1s00]], [[1umx|1umx]], [[1yst|1yst]], [[1z9j|1z9j]], [[1z9k|1z9k]], [[2bnp|2bnp]], [[2bns|2bns]], [[2boz|2boz]], [[2gmr|2gmr]], [[2j8c|2j8c]], [[2j8d|2j8d]], [[2rcr|2rcr]], [[2uws|2uws]], [[4rcr|4rcr]], [[2uwt|2uwt]], [[2uwu|2uwu]], [[2uwv|2uwv]], [[2uww|2uww]], [[2ux3|2ux3]], [[2ux5|2ux5]]</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=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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=2ux4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ux4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ux4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ux4 PDBsum]</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=2ux4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ux4 OCA], [https://pdbe.org/2ux4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ux4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ux4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ux4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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/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/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.  
[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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ux/2ux4_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ux/2ux4_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=2ux4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2ux4" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rhodobacter sphaeroides]]
[[Category: Cereibacter sphaeroides]]
[[Category: Diehm, R]]
[[Category: Large Structures]]
[[Category: Fritzsch, G]]
[[Category: Diehm R]]
[[Category: Koepke, J]]
[[Category: Fritzsch G]]
[[Category: Bacteriochlorophyll]]
[[Category: Koepke J]]
[[Category: Binding positions of the secondary quinone qb]]
[[Category: Cardiolipin]]
[[Category: Chlorophyll]]
[[Category: Chromophore]]
[[Category: Electron transport]]
[[Category: Glucosylgalactosyl diacylglycerol]]
[[Category: Iron]]
[[Category: Magnesium]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Phosphatidylcholine]]
[[Category: Photosynthesis]]
[[Category: Proton translocation pathway]]
[[Category: Reaction center]]
[[Category: Transmembrane]]
[[Category: Transport]]

Latest revision as of 17:56, 13 December 2023

X-ray high resolution structure of the photosynthetic reaction center from Rb. sphaeroides at pH 9 in the charge-separated state, 2nd datasetX-ray high resolution structure of the photosynthetic reaction center from Rb. sphaeroides at pH 9 in the charge-separated state, 2nd dataset

Structural highlights

2ux4 is a 3 chain structure with sequence from Cereibacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.51Å
Ligands:, , , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the photosynthetic reaction-center from Rhodobacter sphaeroides has been determined at four different pH values (6.5, 8.0, 9.0, 10.0) in the neutral and in charge separated states. At pH 8.0, in the neutral state, we obtain a resolution of 1.87 A, which is the best ever reported for the bacterial reaction center protein. Our crystallographic data confirm the existence of two different binding positions of the secondary quinone (QB). We observe a new orientation of QB in its distal position, which shows no ring-flip compared to the orientation in the proximal position. Datasets collected for the different pH values show a pH-dependence of the population of the proximal position. The new orientation of QB in the distal position and the pH-dependence could be confirmed by continuum electrostatics calculations. Our calculations are in agreement with the experimentally observed proton uptake upon charge separation. The high resolution of our crystallographic data allows us to identify new water molecules and external residues being involved in two previously described hydrogen bond proton channels. These extended proton-transfer pathways, ending at either of the two oxo-groups of QB in its proximal position, provide additional evidence that ring-flipping is not required for complete protonation of QB upon reduction.

pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states.,Koepke J, Krammer EM, Klingen AR, Sebban P, Ullmann GM, Fritzsch G J Mol Biol. 2007 Aug 10;371(2):396-409. Epub 2007 May 10. PMID:17570397[1]

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

References

  1. Koepke J, Krammer EM, Klingen AR, Sebban P, Ullmann GM, Fritzsch G. pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states. J Mol Biol. 2007 Aug 10;371(2):396-409. Epub 2007 May 10. PMID:17570397 doi:http://dx.doi.org/10.1016/j.jmb.2007.04.082

2ux4, resolution 2.51Å

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