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Volumn 410, Issue 1, 2011, Pages 52-56

Crystal structure of Pseudomonas aeruginosa PA2196, a putative TetR family transcriptional repressor

Author keywords

Helix turn helix motif; TetR family transcriptional repressor; X ray crystallography

Indexed keywords

PUTATIVE NEUROTRANSMITTER;

EID: 79959378731     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.103     Document Type: Article
Times cited : (6)

References (18)
  • 5
    • 64649105182 scopus 로고    scopus 로고
    • Structures of AcrR and CmeR: insight into the mechanisms of transcriptional repression and multi-drug recognition in the TetR family of regulators
    • Routh M.D., Su C.C., Zhang Q., Yu E.W. Structures of AcrR and CmeR: insight into the mechanisms of transcriptional repression and multi-drug recognition in the TetR family of regulators. Biochim. Biophys. Acta 2009, 1794:844-851.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 844-851
    • Routh, M.D.1    Su, C.C.2    Zhang, Q.3    Yu, E.W.4
  • 7
    • 50249134327 scopus 로고    scopus 로고
    • The uncharacterized transcription factor YdhM is the regulator of the nemA gene encoding N-ethylmaleimide reductase
    • Umezawa Y., Shimada T., Kori A., Yamada K., Ishihama A. The uncharacterized transcription factor YdhM is the regulator of the nemA gene encoding N-ethylmaleimide reductase. J. Bacteriol. 2008, 190:5890-5897.
    • (2008) J. Bacteriol. , vol.190 , pp. 5890-5897
    • Umezawa, Y.1    Shimada, T.2    Kori, A.3    Yamada, K.4    Ishihama, A.5
  • 8
    • 0029868462 scopus 로고    scopus 로고
    • DNA-binding properties of the BetI repressor protein of Escherichia coli: the inducer choline stimulates BetI-DNA complex formation
    • Rkenes T.P., Lamark T., Strom A.R. DNA-binding properties of the BetI repressor protein of Escherichia coli: the inducer choline stimulates BetI-DNA complex formation. J. Bacteriol. 1996, 178:1663-1670.
    • (1996) J. Bacteriol. , vol.178 , pp. 1663-1670
    • Rkenes, T.P.1    Lamark, T.2    Strom, A.R.3
  • 10
    • 0030774268 scopus 로고    scopus 로고
    • Butyrolactone autoregulator receptor protein (BarA) as a transcriptional regulator in Streptomyces virginiae
    • Kinoshita H., Ipposhi H., Okamoto S., Nakano H., Nihira T., Yamada Y. Butyrolactone autoregulator receptor protein (BarA) as a transcriptional regulator in Streptomyces virginiae. J. Bacteriol. 1997, 179:6986-6993.
    • (1997) J. Bacteriol. , vol.179 , pp. 6986-6993
    • Kinoshita, H.1    Ipposhi, H.2    Okamoto, S.3    Nakano, H.4    Nihira, T.5    Yamada, Y.6
  • 11
    • 0028244325 scopus 로고
    • Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
    • Hinrichs W., Kisker C., Duvel M., Muller A., Tovar K., Hillen W., Saenger W. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science 1994, 264:418-420.
    • (1994) Science , vol.264 , pp. 418-420
    • Hinrichs, W.1    Kisker, C.2    Duvel, M.3    Muller, A.4    Tovar, K.5    Hillen, W.6    Saenger, W.7
  • 12
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L., Rosenstrom P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 2010, 38:W545-549.
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 17
    • 0036500260 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR
    • Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A., Brennan R.G. Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR. EMBO J. 2002, 21:1210-1218.
    • (2002) EMBO J. , vol.21 , pp. 1210-1218
    • Schumacher, M.A.1    Miller, M.C.2    Grkovic, S.3    Brown, M.H.4    Skurray, R.A.5    Brennan, R.G.6
  • 18
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins
    • Hendlich M., Rippmann F., Barnickel G. LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J. Mol. Graph Model 1997, 15:359-363, 389.
    • (1997) J. Mol. Graph Model , vol.15 , pp. 359-363
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.