1hx1
From Proteopedia
CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN
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.
About this Structure
1HX1 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. 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 Page seeded by OCA on Fri May 2 19:18:47 2008
