We propose to determine the structure of a complex between the E. coli chaperonin GroEL (Cpn60) and the gp 5 capsid protein of bacteriophage HK97. Suitable crystals have been obtained, they can be flash frozen at -160oC and preliminary data have been collected at CHESS to 3.6 ? resolution. Chaperonins, including members of the Cpn60 family are a ubiuitous class of proteins that assist in protein folding in vivo by binding to partially folded proteins; this prevents aggregation and may unfold off pathway intermediates and direct them back into the correct folding pathway. The gp 5 protein is a natural substrate of GroEL; it is the major capsid protein in the ocosahedral head of the lambdoid bacteriophage HK97. The unit cell parameters are: a = 138.0,b = 270.9, c = 155.4 ?, b = 101.4o. The Space Group is P2. The asymmetric unit contains one 14mer of GroEL and one subunit of the HK97 gp5 protein, i.e. it is the smallest asymmetric unti that could contain a complete complex of this type.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-18
Application #
6339165
Study Section
Project Start
2000-08-15
Project End
2001-08-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
18
Fiscal Year
2000
Total Cost
$13,597
Indirect Cost
Name
Cornell University
Department
Type
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
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