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2uxm

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Revision as of 09:56, 7 February 2016

X-RAY HIGH RESOLUTION STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTER FROM RB. SPHAEROIDES AT PH 10 IN THE CHARGE-SEPARATED STATE, 2ND DATASET

Structural highlights

2uxm is a 3 chain structure with sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , ,
Related:	1aig, 1aij, 1ds8, 1dv3, 1dv6, 1e14, 1e6d, 1f6n, 1fnp, 1fnq, 1jgw, 1jgx, 1jgy, 1jgz, 1jh0, 1k6l, 1k6n, 1kby, 1l9b, 1l9j, 1m3x, 1mps, 1ogv, 1pcr, 1pss, 1pst, 1qov, 1rg5, 1rgn, 1rqk, 1rvj, 1ry5, 1rzh, 1rzz, 1s00, 1umx, 1yst, 1z9j, 1z9k, 2bnp, 2bns, 2boz, 2gmr, 2j8c, 2j8d, 2rcr, 2uws, 2uwt, 2uwu, 2uwv, 2uww, 2ux3, 2ux4, 2ux5, 4rcr, 2uxj, 2uxk, 2uxl
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[RCEH_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEM_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEL_RHOSH] 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

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2uxm"

@@ Line 5: / Line 5: @@
 </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=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='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]], [[2uwt|2uwt]], [[2uwu|2uwu]], [[2uwv|2uwv]], [[2uww|2uww]], [[2ux3|2ux3]], [[2ux4|2ux4]], [[2ux5|2ux5]], [[4rcr|4rcr]], [[2uxj|2uxj]], [[2uxk|2uxk]], [[2uxl|2uxl]]</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=2uxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uxm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uxm RCSB], [http://www.ebi.ac.uk/pdbsum/2uxm PDBsum]</span></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=2uxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uxm OCA], [http://pdbe.org/2uxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uxm RCSB], [http://www.ebi.ac.uk/pdbsum/2uxm PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <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/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=2uxm ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2uxm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2uxm

From Proteopedia

Revision as of 09:56, 7 February 2016

X-RAY HIGH RESOLUTION STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTER FROM RB. SPHAEROIDES AT PH 10 IN THE CHARGE-SEPARATED STATE, 2ND DATASET

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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