Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.84
Classification:CHAPERONE
Release Date:2004-01-20
Deposition Date:2004-01-14
Revision Date:2008-04-29#2011-07-13
Molecular Weight:42747.0
Macromolecule Type:Protein
Residue Count:382
Atom Site Count:2967
DOI:10.2210/pdb1s3x/pdb
Abstract:
The 70 kDa heat shock proteins (Hsp70) are a family of molecular chaperones, which promote protein folding and participate in many cellular functions. The Hsp70 chaperones are composed of two major domains. The N-terminal ATPase domain binds to and hydrolyzes ATP, whereas the C-terminal domain is required for polypeptide binding. Cooperation of both domains is needed for protein folding. The crystal structure of bovine Hsc70 ATPase domain (bATPase) has been determined and, more recently, the crystal structure of the peptide-binding domain of a related chaperone, DnaK, in complex with peptide substrate has been obtained. The molecular chaperone activity and conformational switch are functionally linked with ATP hydrolysis. A high-resolution structure of the ATPase domain is required to provide an understanding of the mechanism of ATP hydrolysis and how it affects communication between C- and N-terminal domains.
Resolution:1.84
Classification:CHAPERONE
Release Date:2004-01-20
Deposition Date:2004-01-14
Revision Date:2008-04-29#2011-07-13
Molecular Weight:42747.0
Macromolecule Type:Protein
Residue Count:382
Atom Site Count:2967
DOI:10.2210/pdb1s3x/pdb
Abstract:
The 70 kDa heat shock proteins (Hsp70) are a family of molecular chaperones, which promote protein folding and participate in many cellular functions. The Hsp70 chaperones are composed of two major domains. The N-terminal ATPase domain binds to and hydrolyzes ATP, whereas the C-terminal domain is required for polypeptide binding. Cooperation of both domains is needed for protein folding. The crystal structure of bovine Hsc70 ATPase domain (bATPase) has been determined and, more recently, the crystal structure of the peptide-binding domain of a related chaperone, DnaK, in complex with peptide substrate has been obtained. The molecular chaperone activity and conformational switch are functionally linked with ATP hydrolysis. A high-resolution structure of the ATPase domain is required to provide an understanding of the mechanism of ATP hydrolysis and how it affects communication between C- and N-terminal domains.
| Date made available | 2004 |
|---|---|
| Publisher | RCSB-PDB |