2w7n
From Proteopedia
Crystal Structure of KorA Bound to Operator DNA: Insight into Repressor Cooperation in RP4 Gene Regulation
Structural highlights
FunctionKORA2_ECOLX In conjunction with KorB, inhibits the transcription of kilA, trfA and korAB operons. In conjunction with KorC is responsible for the negative control of kilC and kilE operons. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedKorA is a global repressor in RP4 which regulates cooperatively the expression of plasmid genes whose products are involved in replication, conjugative transfer and stable inheritance. The structure of KorA bound to an 18-bp DNA duplex that contains the symmetric operator sequence and incorporates 5-bromo-deoxyuridine nucleosides has been determined by multiple-wavelength anomalous diffraction phasing at 1.96-A resolution. KorA is present as a symmetric dimer and contacts DNA via a helix-turn-helix motif. Each half-site of the symmetric operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based on two KorA side chains forming hydrogen bonds to four bases within each operator half-site. KorA has a unique dimerization module shared by the RP4 proteins TrbA and KlcB. We propose that these proteins cooperate with the global RP4 repressor KorB in a similar manner via this dimerization module and thus regulate RP4 inheritance. Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation.,Konig B, Muller JJ, Lanka E, Heinemann U Nucleic Acids Res. 2009 Apr;37(6):1915-24. Epub 2009 Feb 3. PMID:19190096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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