1z2g

From Proteopedia

---

Revision as of 05:05, 21 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1z2g Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Solution structure of apo, oxidized yeast Cox17

Overview

Cox17 is a key mitochondrial copper chaperone involved in the assembly of, cytochrome c oxidase (COX). The NMR solution structure of the oxidized, apoCox17 isoform consists of a coiled-coil conformation stabilized by two, disulfide bonds involving Cys(26)/Cys(57) and Cys(36)/Cys(47). This, appears to be a conserved tertiary fold of a class of proteins, localized, within the mitochondrial intermembrane space, that contain a twin, Cys-x(9)-Cys sequence motif. An isomerization of one disulfide bond from, Cys(26)/Cys(57) to Cys(24)/Cys(57) is required prior to Cu(I) binding to, form the Cu(1)Cox17 complex. Upon further oxidation of the apo-protein, a, form with three disulfide bonds is obtained. The reduction of all, disulfide bonds provides a molten globule form that can convert to an, additional conformer capable of binding up to four Cu(I) ions in a, polycopper cluster. This form of the protein is oligomeric. These, properties are framed within a complete model of mitochondrial import and, COX assembly.

About this Structure

1Z2G is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding., Arnesano F, Balatri E, Banci L, Bertini I, Winge DR, Structure. 2005 May;13(5):713-22. PMID:15893662

Page seeded by OCA on Wed Nov 21 07:12:27 2007