Linked Life Data

6350299

Source:http://linkedlifedata.com/resource/pubmed/id/6350299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1983-10-28
pubmed:abstractText
Using small angle x-ray scattering from solutions of colicin E3-immunity protein complex and the separated proteins, we have measured the radii of gyration of each species. We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact with a radius of gyration of 13.4 +/- 0.1 A. Upon removal of immunity protein from the complex, colicin E3 (form minus immunity protein) undergoes further elongation and dimerizes, such that its radius of gyration increases to 75.6 +/- 3.1 A. Dimerization is not reversed by simple addition of a stoichiometric amount of immunity protein to the E3 solution, even though this is sufficient to block in vitro activity. We suggest that the elongation, and perhaps dimer formation, occurs in vivo, concomitant with membrane translocation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10967-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Dimerization by colicin E3 in the absence of immunity protein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.