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7hsc
From Proteopedia
HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
Overview
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.
About this Structure
7HSC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70., Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER, J Mol Biol. 1999 Jun 25;289(5):1387-403. PMID:10373374 Page seeded by OCA on Sun May 4 22:45:12 2008
