Linked Life Data

19306883

Source:http://linkedlifedata.com/resource/pubmed/id/19306883

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-5-4
pubmed:abstractText
Colicin N is a pore-forming bacteriocin that enters target Escherichia coli cells with the assistance of TolA, a protein in the periplasm of the target cell. The N-terminal domain of the colicin that carries the TolA-binding epitope, the translocation domain (T-domain), is intrinsically disordered. From (1)H-(13)C-(15)N NMR studies of isotopically labeled T-domain interacting with unlabeled TolAIII (the C-terminal domain of TolA), we have identified the TolA-binding epitope and have shown that the extent of its disorder is reduced on binding TolA, although it does not fold into a globular structure with defined secondary structure elements. Residues upstream and downstream of the 27-residue TolA-binding epitope remain disordered in the TolA-bound T-domain as they are in the free T-domain. Filamentous phage also exploits TolAIII to enter target cells, with TolAIII retaining its main secondary structure elements and global fold. In contrast to this, binding of the disordered T-domain of colicin A causes dramatic conformational changes in TolAIII marked by increased flexibility and lack of a rigid tertiary structure consistent with at least partial unfolding of TolAIII, suggesting that bacteriocins and bacteriophages parasitize E. coli using different modes of interaction with TolAIII. We have found that the colicin N T-domain-TolAIII interaction is strikingly similar to the previously described g3p-TolAIII interaction. The fact that both colicin N and filamentous phage exploit TolAIII in a similar manner, with one being a bacterial intrinsically disordered protein and the other being a viral structurally well-ordered protein, suggests that these represent a good example of convergent evolution at the molecular level.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
388
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
880-93
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
A common interaction for the entry of colicin N and filamentous phage into Escherichia coli.
pubmed:affiliation
Center for Molecular and Structural Biochemistry, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't