2uxk
|
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 ... [(full description)]
About this StructureAbout this Structure
2UXK is a [Protein complex] structure of sequences from [Rhodobacter sphaeroides] with PO4, FE, BCL, LDA, BPH, UQ2, HTO, U10, SPO, CDN and GOL as [ligands]. Structure known Active Site: AC1. 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 Tue Oct 30 17:39:43 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Protein complex
- Rhodobacter sphaeroides
- Diehm, R.
- Fritzsch, G.
- Koepke, J.
- BCL
- BPH
- CDN
- FE
- GOL
- HTO
- LDA
- PO4
- SPO
- U10
- UQ2
- Bacteriochlorophyll
- Binding positions of the secondary quinone qb
- Cardiolipin
- Chlorophyll
- Chromophore
- Electron transport
- Iron
- Magnesium
- Membrane
- Metal-binding
- Photosynthesis
- Proton translocation pathways
- Reaction center
- Transmembrane
- Transport