CRYSTAL STRUCTURE OF MOLECULAR CHAPERONE, HSC20

$143,176P41FY2002RRNIH

Stanford University, Stanford CA

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Abstract

Molecular chaperones play key roles in protein folding, transport across membranes, and in response to stressful stimuli. Hsc20 is a DnaJ-type "co-chaperone" protein encoded in a recently discovered operon in E. coli which also encodes a DnaK/hsp70-type chaperone. To date, no structure for a DnaJ co-chaperone has been determined. We have recently succeeded in overexpresing, purifying and crystallizing Hsc20. Thus, Hsc20 could provide the first complete high resolution crystal structure for proteins of this class.

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