1yuw | pdb_00001yuw
crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant
|
Overview
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.
About this Structure
1YUW is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis of interdomain communication in the Hsc70 chaperone., Jiang J, Prasad K, Lafer EM, Sousa R, Mol Cell. 2005 Nov 23;20(4):513-24. PMID:16307916
Page seeded by OCA on Wed Nov 21 07:03:57 2007
