1S3X
The crystal structure of the human Hsp70 ATPase domain
Summary for 1S3X
| Entry DOI | 10.2210/pdb1s3x/pdb |
| Related | 1HJO 3HSC |
| Descriptor | Heat shock 70 kDa protein 1, PHOSPHATE ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | hsp70, atpase, molecular chaperone, chaperone |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P08107 |
| Total number of polymer chains | 1 |
| Total formula weight | 42747.00 |
| Authors | Sriram, M.,Osipiuk, J.,Freeman, B.,Morimoto, R.I.,Joachimiak, A. (deposition date: 2004-01-14, release date: 2004-01-20, Last modification date: 2023-08-23) |
| Primary citation | SRIRAM, M.,OSIPIUK, J.,FREEMAN, B.,MORIMOTO, R.I.,JOACHIMIAK, A. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain Structure, 5:403-414, 1997 Cited by PubMed 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. PubMed: 9083109DOI: 10.1016/S0969-2126(97)00197-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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