Linked Life Data

12555855

Source:http://linkedlifedata.com/resource/pubmed/id/12555855

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2003-1-30
pubmed:databankReference
pubmed:abstractText
Colicin E9 is a 61 kDa antibacterial protein secreted by E. coli. In order for it to enter the cytoplasm of susceptible bacteria and kill them by hydrolysing their DNA, the colicin must first interact with an outer membrane receptor on the target cell, BtuB, and a translocation pathway involving Tol proteins. The receptor binding, translocation and DNase functions of colicin E9 are housed in discrete structural domains, which have been independently expressed and characterized. The minimal receptor-binding domain is a 76 amino acid protein (min-R). X-ray structure determination of a related colicin shows its receptor-binding-domain to have a helical hairpin structure (S. Soelaiman, K. Jakes, N. Wu, C. Li and M. Shoham, Molecular Cell. 2001, 8, 1053). Our solution NMR studies of min-R have confirmed it has a helical hairpin structure, and shown it has multiple slowly interchanging conformers and a flexible inter-helix loop. A plausible interpretation of these data is that in solution the helical hairpin can adopt a variety of structures differing in the spatial relationship of the two helices. A possible biological role for this involves the hairpin opening during translocation into bacteria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1359-6640
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-62; discussion 171-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Structural dynamics of the receptor-binding domain of colicin E9.
pubmed:affiliation
School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't