7HSC
HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
Summary for 7HSC
| Entry DOI | 10.2210/pdb7hsc/pdb |
| NMR Information | BMRB: 4497,4599 |
| Descriptor | PROTEIN (HEAT SHOCK COGNATE 70 KD PROTEIN 1) (1 entity in total) |
| Functional Keywords | molecular chaperone, hsp70, peptide binding, protein folding |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasm (By similarity): P63018 |
| Total number of polymer chains | 1 |
| Total formula weight | 17558.75 |
| Authors | Morshauser, R.C.,Hu, W.,Wang, H.,Pang, Y.,Flynn, G.C.,Zuiderweg, E.R.P. (deposition date: 1999-05-03, release date: 1999-05-10, Last modification date: 2023-12-27) |
| Primary citation | Morshauser, R.C.,Hu, W.,Wang, H.,Pang, Y.,Flynn, G.C.,Zuiderweg, E.R. High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. J.Mol.Biol., 289:1387-1403, 1999 Cited by PubMed Abstract: The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540 (18 kDa) and is necessary for the binding of the chaperone with substrate proteins and peptides. The high-resolution NMR solution structure is based on 4150 experimental distance constraints leading to an average root-mean-square precision of 0.38 A for the backbone atoms and 0.76 A for all atoms in the beta-sandwich sub-domain. The protein is observed to bind residue Leu539 in its hydrophobic substrate-binding groove by intramolecular interaction. The position of a helical latch differs dramatically from what is observed in the crystal and solution structures of the homologous prokaryotic chaperone DnaK. In the Hsc70 structure, the helix lies in a hydrophobic groove and is anchored by a buried salt-bridge. Residues involved in this salt-bridge appear to be important for the allosteric functioning of the protein. A mechanism for interdomain allosteric modulation of substrate-binding is proposed. It involves large-scale movements of the helical domain, redefining the location of the hinge area that enables such motions. PubMed: 10373374DOI: 10.1006/jmbi.1999.2776 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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