Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors
| Autor: | Ismail Moarefi, Clemens Scheufler, Jörg Höhfeld, F. Ulrich Hartl, Holger Sondermann, Christine Schneider |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular BAG domain Protein Conformation ATPase Molecular Sequence Data Biology Crystallography X-Ray Protein Structure Secondary BAG1 Evolution Molecular Nucleotide exchange factor Adenosine Triphosphate Bacterial Proteins Heat shock protein Animals Humans Protein Isoforms HSP70 Heat-Shock Proteins Nucleotide Amino Acid Sequence Heat-Shock Proteins Adenosine Triphosphatases chemistry.chemical_classification Multidisciplinary Escherichia coli Proteins Hydrolysis HSC70 Heat-Shock Proteins Protein Structure Tertiary Hsp70 Adenosine Diphosphate DNA-Binding Proteins Biochemistry chemistry Chaperone (protein) biology.protein Biophysics Cattle Carrier Proteins Transcription Factors |
| Zdroj: | Science. 291:1553-1557 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1057268 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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