TY - JOUR
T1 - 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
AU - Doi, Akihiro
AU - Okajima, Toshihide
AU - Gotoh, Yasuhiro
AU - Tanizawa, Katsuyuki
AU - Utsumi, Ryutaro
N1 - Funding Information:
This work was supported by the Research and Development Program for New Bio-Industry Initiatives (2006–2010) of the Bio-Oriented Technology Research Advancement Institution (BRAIN) of Japan. The radiation experiment was done at BL44XU in SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI).
Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77957359441&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77957359441&partnerID=8YFLogxK
U2 - 10.1271/bbb.100307
DO - 10.1271/bbb.100307
M3 - Article
C2 - 20834167
AN - SCOPUS:77957359441
SN - 0916-8451
VL - 74
SP - 1901
EP - 1907
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 9
ER -
