Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2004-7-19
pubmed:databankReference
pubmed:abstractText
The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of beta-strands in the N-terminal alphabeta loop that align with the major beta-strands to form a continuous 7-stranded antiparallel beta-sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the alphabeta loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31599-605
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
pubmed:affiliation
Department of Biological Sciences, National University of Singapore, Singapore 117543.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't