1YUW

crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant

Summary for 1YUW

• Entry DOI: 10.2210/pdb1yuw/pdb
• Related: 3HSC 7HSC
• Descriptor: Heat shock cognate 71 kDa protein (2 entities in total)
• Functional Keywords: chaperone
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm : P19120
• Total number of polymer chains: 1
• Total formula weight: 60978.87

Authors

Jiang, J.,Lafer, E.M.,Prasad, K.,Sousa, R. (deposition date: 2005-02-14, release date: 2005-10-04, Last modification date: 2024-02-14)

Primary citation

Jiang, J.,Prasad, K.,Lafer, E.M.,Sousa, R.
Structural basis of interdomain communication in the Hsc70 chaperone
Mol.Cell, 20:513-524, 2005

PubMed Abstract: 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.

PubMed: 16307916
DOI: 10.1016/j.molcel.2005.09.028

Experimental method

X-RAY DIFFRACTION (2.6 Å)