Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-7-16
pubmed:abstractText
OmpR, a protein that regulates expression of outer membrane porin proteins in enteric bacteria, belongs to a large family of transcription factors. These transcription factors bind DNA and interact productively with RNA polymerase to activate transcription. The two functions, DNA-binding and transcriptional activation, have been localized within the 100 amino acid DNA-binding domain that characterizes members of the OmpR family. Both DNA binding and transcriptional activation by OmpR related proteins have remained poorly understood for lack of structural information or lack of sequence homology with transcription factors of known three-dimensional structure. The recently determined crystal structures of the Escherichia coli OmpR DNA-binding domain (OmpRc) have defined a new subfamily of "winged-helix-turn-helix" DNA-binding proteins. Structural elements of OmpRc can be assigned functional roles by analogy to other winged-helix DNA-binding proteins. A structure based sequence analysis of the OmpR family of transcription factors indicates specific roles for all conserved amino acid residues. Mutagenesis studies performed on several members of this family, OmpR, PhoB, ToxR and VirG, can now be interpreted with respect to the structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
301-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Structural relationships in the OmpR family of winged-helix transcription factors.
pubmed:affiliation
Center for Advanced Biotechnology and Medicine and Dept. of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway 08854, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't