Document Detail

Identification and characterization of the domain structure of bacteriophage P22 coat protein.
MedLine Citation:
PMID:  10545185     Owner:  NLM     Status:  MEDLINE    
The bacteriophage P22 serves as a model for assembly of icosahedral dsDNA viruses. The P22 procapsid, which constitutes the precursor for DNA packaging, is built from 420 copies of a single coat protein with the aid of stoichiometric amounts of scaffolding protein. Upon DNA entry, the procapsid shell expands and matures into a stable virion. It was proposed that expansion is mediated by hinge bending and domain movement. We have used limited proteolysis to map the dynamic stability of the coat protein domain structures. The coat protein monomer is susceptible to proteolytic digestion, but limited proteolysis by small quantities of elastase or chymotrypsin yielded two metastable fragments (domains). The N-terminal domain (residues 1-180) is linked to the C-terminal domain (residues 205-429) by a protease-susceptible loop (residues 180-205). The two domains remain associated after the loop cleavage. Although only a small change of secondary structure results from the loop cleavage, both tertiary interdomain contacts and subunit thermostability are diminished. The intact loop is also required for assembly of the monomeric coat protein into procapsids. Upon assembly, coat protein becomes largely protease-resistant, baring cleavage within the loop region of about half of the subunits. Loop cleavage decreases the stability of the procapsids and facilitates heat-induced shell expansion. Upon expansion, the loop becomes protease-resistant. Our data suggest the loop region becomes more ordered during assembly and maturation and thereby plays an important role in both of these stages.
J Lanman; R Tuma; P E Prevelige
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  38     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1999 Nov 
Date Detail:
Created Date:  1999-12-22     Completed Date:  1999-12-22     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  14614-23     Citation Subset:  IM    
Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35205, USA.
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MeSH Terms
Bacteriophage P22 / chemistry*,  growth & development
Capsid / chemistry*
Drug Stability
Pancreatic Elastase
Peptide Fragments / chemistry
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Grant Support
Reg. No./Substance:
0/Peptide Fragments; EC Elastase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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