X-ray crystal structure of the DNA-binding domain of response regulator WalR essential to the cell viability of Staphyloccus aureus and interaction with target DNA

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  • DOI Akihiro
    Department of Bioscience, Graduate School of Agriculture, Kinki University
  • OKAJIMA Toshihide
    Institute of Scientific and Industrial Research, Osaka University
  • GOTOH Yasuhiro
    Department of Bioscience, Graduate School of Agriculture, Kinki University
  • TANIZAWA Katsuyuki
    Institute of Scientific and Industrial Research, Osaka University
  • UTSUMI Ryutaro
    Department of Bioscience, Graduate School of Agriculture, Kinki University

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タイトル別名
  • X-Ray Crystal Structure of the DNA-Binding Domain of Response Regulator WalR Essential to the Cell Viability of Staphylococcus aureus and Interaction with Target DNA
  • X-Ray Crystal Structure of the DNA-Binding Domain of Response Regulator WalR Essential to the Cell Viability of <i>Staphylococcus aureus</i> and Interaction with Target DNA

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A bacterial two-component signal transduction system, WalK/WalR, is essential to the cell viability of Gram-positive bacteria and is therefore a potential target for the development of a new class of antibiotics. We have solved the X-ray crystal structure of the DNA-binding domain of the response regulator WalR (WalRc) from a Gram-positive pathogen Staphylococcus aureus, currently causing serious problems in public health through the acquisition of multi-drug resistance. The structure contains a winged helix-turn-helix motif and closely resembles those of WalRs of Bacillus subtilis and Enterococcus faecalis, and also that of PhoB of Escherichia coli. Gel mobility shift assays with mutant WalRs revealed specific interactions of WalR with the target DNA, as elaborated by in silico modeling of the WalRc-DNA complex.

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