3cxh: Difference between revisions

Revision as of 22:24, 2 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:3cxh.png

Template:STRUCTURE 3cxh

Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.

Template:ABSTRACT PUBMED 18390544

About this StructureAbout this Structure

3CXH is a Protein complex structure of sequences from Mus musculus and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer., Solmaz S, Hunte C, J Biol Chem. 2008 Apr 4;. PMID:18390544

Page seeded by OCA on Wed Jul 2 22:24:41 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:3cxh.jpg|left|200px]]
+{{Seed}}
+[[Image:3cxh.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3cxh|  PDB=3cxh  |  SCENE=  }}
-'''Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.'''
+===Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.===
-==Overview==
+<!--
-In cellular respiration, cytochrome c transfers electrons from cytochrome bc1 complex (complex III) to cytochrome c oxidase by transiently binding to the membrane proteins. Here, we report the structure of isoform-1 cytochrome c bound to cytochrome bc1 complex at 1.9-A resolution in reduced state. The dimer structure is asymmetric. Monovalent cytochrome c binding is correlated with conformational changes of the Rieske head domain and subunit QCR6p and with a higher number of interfacial water molecules bound to cytochrome c1. Pronounced hydration and a 'mobility mismatch' at the interface with disordered charged residues on the cytochrome c side are favourable for transient binding. Within the hydrophobic interface, a minimal core was identified by comparison with the novel structure of the complex with bound isoform-2 cytochrome c. Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_18390544}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18390544 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18390544}}
 ==About this Structure==
@@ Line 45: / Line 49: @@
 [[Category: Transit peptide]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:34:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:24:41 2008''