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Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation

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Item Type:Article
Title:Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation
Creators Name:Koenig, B. and Mueller, J.J. and Lanka, E. and Heinemann, U.
Abstract:KorA 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.
Keywords:Amino Acid Sequence, Bacterial Proteins, Binding Sites, X-Ray Crystallography, Bacterial DNA, DNA-Binding Proteins, Bacterial Gene Expression Regulation, Molecular Models, Molecular Sequence Data, Nucleic Acid Conformation, Genetic Operator Regions, Plasmids, Protein Multimerization, Tertiary Protein Structure, Repressor Proteins
Source:Nucleic Acids Research
Publisher:Oxford University Press
Page Range:1915-1924
Date:April 2009
Official Publication:https://doi.org/10.1093/nar/gkp044
PubMed:View item in PubMed

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