Molecular chaperons of the Hsp70 family bind unfolded polypeptide substrates to stabilize or alter their conformation and hydrolyze ATP to facilitate polypeptide release. The ATP hydrolysis of Hsp70 is regulated by another protein chaperon family Hsp40. It has been reported that Hsp40 my bind polypeptides with secondary structure, interact directly with Hsp70 and stimulate the ATP hydrolysis of Hsp70. SIS1 is a member of Hsp40 protein family in Yeast Saccharomyces cerevisiae and essential for cell viability. We have crystallized the protein SIS1 recently, the crystals diffract to 2.7 E. Selenomethionyl SIS1 has been expressed and purified from E. coli strain B834. Similar crystals are obtained using the same conditions. This proposal requests beamtime to use the MAD method to solve the 3-D crystal structure of protein Hsp40.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6119592
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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