1hx1

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Revision as of 15:17, 12 November 2007

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spinqualitylabelsall models 1hx1, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Bag (Bcl2-associated athanogene) domains occur in a class of cofactors of, the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family., Binding of the Bag domain to the Hsp70 adenosine triphosphatase (ATPase), domain promotes adenosine 5'-triphosphate-dependent release of substrate, from Hsp70 in vitro. In a 1.9 angstrom crystal structure of a complex with, the ATPase of the 70-kilodalton heat shock cognate protein (Hsc70), the, Bag domain forms a three-helix bundle, inducing a conformational switch in, the ATPase that is incompatible with nucleotide binding. The same switch, is observed in the bacterial Hsp70 homolog DnaK upon binding of the, structurally unrelated nucleotide exchange factor GrpE. Thus, functional, convergence has allowed proteins with different architectures to trigger a, conserved conformational shift in Hsp70 that leads to nucleotide exchange.

Disease

Known disease associated with this structure: Camptodactyly-arthropathy-coxa vara-pericarditis syndrome OMIM:[604283]

About this Structure

1HX1 is a Protein complex structure of sequences from Bos taurus and Homo sapiens with TRS as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors., Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I, Science. 2001 Feb 23;291(5508):1553-7. PMID:11222862

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