Linked Life Data

17308310

Source:http://linkedlifedata.com/resource/pubmed/id/17308310

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2007-4-23
pubmed:databankReference
pubmed:abstractText
The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12353-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.
pubmed:affiliation
Institute of Genetics, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't