Understanding the evolution of the coat protein fold using P22-like phages
EMSL Project ID
51064
Abstract
Despite very low sequence homology, the major capsid proteins of dsDNA bacteriophages, some archaeal viruses and the herpesviruses, share a common structural motif - the HK97-fold. My group is investigating how evolution has affected the structure and function of this fold. Bacteriophage P22 belongs to a family of at least 151 distantly related bacteriophages. The coat proteins of these phages fall into three classes based on sequence identity: P22-like, CUS-3-like and Sf6-like. However, the coat proteins of phages P22, Sf6, and CUS-3 are only ~15-30% identical. High-resolution cryoEM structures are available for P22 and Sf6 capsids, but not yet for CUS-3. Without the high-resolution structure for CUS-3, we are left to deduce which coat protein interactions are important for CUS-3 capsid assembly and stabilization. We propose to do the high-resolution cryoEM structure of CUS-3 phages and procapsids.
Project Details
Start Date
2019-10-15
End Date
2020-07-15
Status
Closed
Released Data Link
Team
Principal Investigator
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