1HX1

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

Summary for 1HX1

• Entry DOI: 10.2210/pdb1hx1/pdb
• Descriptor: Heat shock 70 kDa protein 8, BAG family molecular chaperone regulator 1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: protein-protein complex, apoptosis, protein folding, molecular chaperone, nucleotide exchange factor, chaperone-chaperone inhibitor complex, chaperone/chaperone inhibitor
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow); More
• Total number of polymer chains: 2
• Total formula weight: 57788.40

Authors

Sondermann, H.,Scheufler, C.,Moarefi, I. (deposition date: 2001-01-11, release date: 2001-03-07, Last modification date: 2019-12-18)

Primary citation

Sondermann, H.,Scheufler, C.,Schneider, C.,Hohfeld, J.,Hartl, F.U.,Moarefi, I.
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors.
Science, 291:1553-1557, 2001

PubMed Abstract: 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.

PubMed: 11222862
DOI: 10.1126/science.1057268

Experimental method

X-RAY DIFFRACTION (1.9 Å)