2uxk: Difference between revisions

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==About this Structure==
==About this Structure==
2UXK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=LDA:'>LDA</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=UQ2:'>UQ2</scene>, <scene name='pdbligand=HTO:'>HTO</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPO:'>SPO</scene>, <scene name='pdbligand=CDN:'>CDN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain H'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXK OCA].  
2UXK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=LDA:'>LDA</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=UQ2:'>UQ2</scene>, <scene name='pdbligand=HTO:'>HTO</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPO:'>SPO</scene>, <scene name='pdbligand=CDN:'>CDN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+H'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXK OCA].  


==Reference==
==Reference==
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[[Category: transport]]
[[Category: transport]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:48:08 2008''

Revision as of 11:48, 3 February 2008

File:2uxk.jpg


2uxk, resolution 2.31Å

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

OverviewOverview

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 (Q(B)). We observe a new orientation of, Q(B) 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 Q(B) 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 Q(B) in its proximal position, provide additional evidence that, ring-flipping is not required for complete protonation of Q(B) upon, reduction.

About this StructureAbout this Structure

2UXK is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , , , , , and as ligands. Known structural/functional Site: . 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

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