2fyn: Difference between revisions

Revision as of 12:11, 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:2fyn.png

Template:STRUCTURE 2fyn

Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complexCrystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex

Template:ABSTRACT PUBMED 16924113

About this StructureAbout this Structure

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

ReferenceReference

Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex., Esser L, Gong X, Yang S, Yu L, Yu CA, Xia D, Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13045-50. Epub 2006 Aug 21. PMID:16924113

Page seeded by OCA on Mon Jul 28 12:11:47 2008

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

OCA

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-'''Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex'''
+===Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex===
-==Overview==
+<!--
-In the cytochrome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites constitutes a key component of the mechanism that achieves the separation of the two electrons in a substrate molecule at the quinol oxidation (Q(o)) site. The question remaining is how the motion of ISP is controlled so that only one electron enters the thermodynamically favorable chain via ISP. An analysis of eight structures of mitochondrial bc(1) with bound Q(o) site inhibitors revealed that the presence of inhibitors causes a bidirectional repositioning of the cd1 helix in the cytochrome b subunit. As the cd1 helix forms a major part of the ISP binding crater, any positional shift of this helix modulates the ability of cytochrome b to bind ISP. The analysis also suggests a mechanism for reversal of the ISP fixation when the shape complementarity is significantly reduced after a positional reorientation of the reaction product quinone. The importance of shape complementarity in this mechanism was confirmed by functional studies of bc(1) mutants and by a structure determination of the bacterial form of bc(1). A mechanism for the high fidelity of the bifurcated electron transfer is proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16924113}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16924113 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16924113}}
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 [[Category: Functional dimer]]
 [[Category: Transmembrane helice]]
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