The solution structure of bacteriophage λ protein W, a small morphogenetic protein possessing a novel fold

Protein W (gpW) from bacteriophage λ is required for the stabilization of DNA within the phage head and for attachment of tails onto the head during morphogenesis. Although comprised of only 68 residues, it likely interacts with at least two other proteins in the mature phage and with DNA. Thus, gpW...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular biology 2001-04, Vol.308 (1), p.9-14
Main Authors: Maxwell, Karen L, Yee, Adelinda A, Booth, Valerie, Arrowsmith, Cheryl H, Gold, Marvin, Davidson, Alan R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteriophage lambda - chemistry
bacteriophage λ
connector
glycoprotein W
head morphogenesis
Models, Molecular
Molecular Sequence Data
NMR structure
Nuclear Magnetic Resonance, Biomolecular
Phage l
Protein Folding
Protein Structure, Quaternary
Protein Structure, Secondary
protein W
Sequence Alignment
Solutions
Thermodynamics
Viral Structural Proteins - chemistry
Viral Structural Proteins - metabolism
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Protein W (gpW) from bacteriophage λ is required for the stabilization of DNA within the phage head and for attachment of tails onto the head during morphogenesis. Although comprised of only 68 residues, it likely interacts with at least two other proteins in the mature phage and with DNA. Thus, gpW is an intriguing subject for detailed structural studies. We have determined its solution structure using NMR spectroscopy and have found it to possesses a novel fold consisting of two α-helices and a single two-stranded β-sheet arranged around a well-packed hydrophobic core. The 14 C-terminal residues of gpW, which are essential for function, are unstructured in solution.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.2001.4582