Linked Life Data

11302702

Source:http://linkedlifedata.com/resource/pubmed/id/11302702

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-4-16
pubmed:databankReference
pubmed:abstractText
Protein W (gpW) from bacteriophage lambda 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 alpha-helices and a single two-stranded beta-sheet arranged around a well-packed hydrophobic core. The 14 C-terminal residues of gpW, which are essential for function, are unstructured in solution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
308
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-14
pubmed:dateRevised
2001-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold.
pubmed:affiliation
Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article