Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.6
Classification:CHAPERONE
Release Date:2005-10-04
Deposition Date:2005-02-14
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:60978.87
Macromolecule Type:Protein
Residue Count:554
Atom Site Count:4282
DOI:10.2210/pdb1yuw/pdb
Abstract:
Hsp70 family proteins are highly conserved chaperones involved in protein folding, degradation, targeting and translocation, and protein complex remodeling. They are comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding to the NBD alters SBD conformation and substrate binding kinetics, but an understanding of the mechanism of interdomain communication has been hampered by the lack of a crystal structure of an intact chaperone. We report here the 2.6 angstroms structure of a functionally intact bovine Hsc70 (bHsc70) and a mutational analysis of the observed interdomain interface and the immediately adjacent interdomain linker. This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the interdomain linker invades and disrupts the interdomain interface when ATP binds.
Resolution:2.6
Classification:CHAPERONE
Release Date:2005-10-04
Deposition Date:2005-02-14
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:60978.87
Macromolecule Type:Protein
Residue Count:554
Atom Site Count:4282
DOI:10.2210/pdb1yuw/pdb
Abstract:
Hsp70 family proteins are highly conserved chaperones involved in protein folding, degradation, targeting and translocation, and protein complex remodeling. They are comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD). ATP binding to the NBD alters SBD conformation and substrate binding kinetics, but an understanding of the mechanism of interdomain communication has been hampered by the lack of a crystal structure of an intact chaperone. We report here the 2.6 angstroms structure of a functionally intact bovine Hsc70 (bHsc70) and a mutational analysis of the observed interdomain interface and the immediately adjacent interdomain linker. This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the interdomain linker invades and disrupts the interdomain interface when ATP binds.
| Date made available | 2005 |
|---|---|
| Publisher | RCSB-PDB |