Publication Date:
2001-02-27
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sondermann, H -- Scheufler, C -- Schneider, C -- Hohfeld, J -- Hartl, F U -- Moarefi, I -- New York, N.Y. -- Science. 2001 Feb 23;291(5508):1553-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max-Planck-Institut fur Biochemie, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11222862" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Diphosphate/metabolism
;
Adenosine Triphosphatases/*chemistry/*metabolism
;
Adenosine Triphosphate/metabolism
;
Amino Acid Sequence
;
Animals
;
Bacterial Proteins/chemistry/metabolism
;
Carrier Proteins/*chemistry/*metabolism
;
Cattle
;
Crystallography, X-Ray
;
DNA-Binding Proteins
;
*Escherichia coli Proteins
;
Evolution, Molecular
;
HSC70 Heat-Shock Proteins
;
HSP70 Heat-Shock Proteins/*chemistry/*metabolism
;
Heat-Shock Proteins/chemistry/metabolism
;
Humans
;
Hydrolysis
;
Models, Molecular
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Isoforms
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Transcription Factors
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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