2ux4: Difference between revisions

Revision as of 11:48, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ux4.png

Template:STRUCTURE 2ux4

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

Template:ABSTRACT PUBMED 17570397

About this StructureAbout this Structure

2UX4 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 11:48:10 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ux4.jpg|left|200px]]
+{{Seed}}
+[[Image:2ux4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ux4|  PDB=2ux4  |  SCENE=  }}
-'''X-RAY HIGH RESOLUTION STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTER FROM RB. SPHAEROIDES AT PH 9 IN THE CHARGE-SEPARATED STATE, 2ND DATASET'''
+===X-RAY HIGH RESOLUTION STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTER FROM RB. SPHAEROIDES AT PH 9 IN THE CHARGE-SEPARATED STATE, 2ND DATASET===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17570397}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17570397 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17570397}}
 ==About this Structure==
@@ Line 42: / Line 46: @@
 [[Category: Transmembrane]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:42:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:48:10 2008''