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Volumn 110, Issue 44, 2013, Pages 17820-17825

Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRATE AMINOTRANSFERASE; 4 AMINOBUTYRIC ACID RECEPTOR;

EID: 84887047300     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1315887110     Document Type: Article
Times cited : (57)

References (19)
  • 1
    • 0037066712 scopus 로고    scopus 로고
    • Subdivision of the helix-Turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies
    • Rigali S, Derouaux A, Giannotta F, Dusart J (2002) Subdivision of the helix-Turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J Biol Chem 277(15):12507-12515.
    • (2002) J Biol Chem , vol.277 , Issue.15 , pp. 12507-12515
    • Rigali, S.1    Derouaux, A.2    Giannotta, F.3    Dusart, J.4
  • 2
    • 0036062693 scopus 로고    scopus 로고
    • GabR, a member of a novel protein family, regulates the utilization of gamma-aminobutyrate in Bacillus subtilis
    • Belitsky BR, Sonenshein AL (2002) GabR, a member of a novel protein family, regulates the utilization of gamma-aminobutyrate in Bacillus subtilis. Mol Microbiol 45(2): 569-583.
    • (2002) Mol Microbiol , vol.45 , Issue.2 , pp. 569-583
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 3
    • 80755188947 scopus 로고    scopus 로고
    • Genomic distribution and heterogeneity of MocR-like transcriptional factors containing a domain belonging to the superfamily of the pyridoxal-5α-phosphate dependent enzymes of fold type i
    • Bramucci E, Milano T, Pascarella S (2011) Genomic distribution and heterogeneity of MocR-like transcriptional factors containing a domain belonging to the superfamily of the pyridoxal-5α-phosphate dependent enzymes of fold type I. Biochem Biophys Res Commun 415(1):88-93.
    • (2011) Biochem Biophys Res Commun , vol.415 , Issue.1 , pp. 88-93
    • Bramucci, E.1    Milano, T.2    Pascarella, S.3
  • 4
    • 0021634693 scopus 로고
    • Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure
    • Kirsch JF, et al. (1984) Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol 174(3):497-525.
    • (1984) J Mol Biol , vol.174 , Issue.3 , pp. 497-525
    • Kirsch, J.F.1
  • 5
    • 0343851637 scopus 로고    scopus 로고
    • The manifold of vitamin B6 dependent enzymes
    • Schneider G, Käck H, Lindqvist Y (2000) The manifold of vitamin B6 dependent enzymes. Structure 8(1):R1-R6.
    • (2000) Structure , vol.8 , Issue.1
    • Schneider, G.1    Käck, H.2    Lindqvist, Y.3
  • 6
    • 3042561987 scopus 로고    scopus 로고
    • Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase domains, is a PLP-dependent transcriptional regulator
    • Belitsky BR (2004) Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase domains, is a PLP-dependent transcriptional regulator. J Mol Biol 340(4): 655-664.
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 655-664
    • Belitsky, B.R.1
  • 7
    • 68949162019 scopus 로고    scopus 로고
    • Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alphaaminoadipate aminotransferase from Thermus thermophilus
    • Ouchi T, Tomita T, Miyagawa T, Kuzuyama T, Nishiyama M (2009) Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alphaaminoadipate aminotransferase from Thermus thermophilus. Biochem Biophys Res Commun 388(1):21-27.
    • (2009) Biochem Biophys Res Commun , vol.388 , Issue.1 , pp. 21-27
    • Ouchi, T.1    Tomita, T.2    Miyagawa, T.3    Kuzuyama, T.4    Nishiyama, M.5
  • 9
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • Eliot AC, Kirsch JF (2004) Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations. Annu Rev Biochem 73:383-415.
    • (2004) Annu Rev Biochem , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 10
    • 0024471943 scopus 로고
    • 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli
    • Smith DL, Almo SC, Toney MD, Ringe D (1989) 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry 28(20):8161-8167.
    • (1989) Biochemistry , vol.28 , Issue.20 , pp. 8161-8167
    • Smith, D.L.1    Almo, S.C.2    Toney, M.D.3    Ringe, D.4
  • 11
    • 78651285748 scopus 로고    scopus 로고
    • Cdd: A Conserved Domain Database for the functional annotation of proteins
    • Database issue
    • Marchler-Bauer A, et al. (2011) CDD: A Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Res 39(Database issue):D225-D229.
    • (2011) Nucleic Acids Res , vol.39
    • Marchler-Bauer, A.1
  • 12
    • 0035901537 scopus 로고    scopus 로고
    • The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR
    • van Aalten DM, DiRusso CC, Knudsen J (2001) The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR. EMBO J 20(8):2041-2050.
    • (2001) EMBO J , vol.20 , Issue.8 , pp. 2041-2050
    • Van Aalten, D.M.1    Dirusso, C.C.2    Knudsen, J.3
  • 13
    • 0030692787 scopus 로고    scopus 로고
    • Characterization of the fatty acid-responsive transcription factor FadR. Biochemical and genetic analyses of the native conformation and functional domains
    • Raman N, Black PN, DiRusso CC (1997) Characterization of the fatty acid-responsive transcription factor FadR. Biochemical and genetic analyses of the native conformation and functional domains. J Biol Chem 272(49):30645-30650.
    • (1997) J Biol Chem , vol.272 , Issue.49 , pp. 30645-30650
    • Raman, N.1    Black, P.N.2    Dirusso, C.C.3
  • 14
    • 0347052772 scopus 로고    scopus 로고
    • Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5α-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin
    • Storici P, et al. (2004) Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5α-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin. J Biol Chem 279(1):363-373.
    • (2004) J Biol Chem , vol.279 , Issue.1 , pp. 363-373
    • Storici, P.1
  • 15
    • 24644442264 scopus 로고    scopus 로고
    • Dual substrate recognition of aminotransferases
    • Hirotsu K, Goto M, Okamoto A, Miyahara I (2005) Dual substrate recognition of aminotransferases. Chem Rec 5(3):160-172.
    • (2005) Chem Rec , vol.5 , Issue.3 , pp. 160-172
    • Hirotsu, K.1    Goto, M.2    Okamoto, A.3    Miyahara, I.4
  • 16
    • 16844384577 scopus 로고    scopus 로고
    • Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica
    • Grose JH, Bergthorsson U, Roth JR (2005) Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica. J Bacteriol 187(8):2774-2782.
    • (2005) J Bacteriol , vol.187 , Issue.8 , pp. 2774-2782
    • Grose, J.H.1    Bergthorsson, U.2    Roth, J.R.3
  • 17
    • 0032521544 scopus 로고    scopus 로고
    • Adaptation of an enzyme to regulatory function: Structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase
    • Tomchick DR, Turner RJ, Switzer RL, Smith JL (1998) Adaptation of an enzyme to regulatory function: Structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase. Structure 6(3):337-350.
    • (1998) Structure , vol.6 , Issue.3 , pp. 337-350
    • Tomchick, D.R.1    Turner, R.J.2    Switzer, R.L.3    Smith, J.L.4
  • 18
    • 0037924464 scopus 로고    scopus 로고
    • The purine repressor of Bacillus subtilis: A novel combination of domains adapted for transcription regulation
    • Sinha SC, et al. (2003) The purine repressor of Bacillus subtilis: A novel combination of domains adapted for transcription regulation. J Bacteriol 185(14):4087-4098.
    • (2003) J Bacteriol , vol.185 , Issue.14 , pp. 4087-4098
    • Sinha, S.C.1
  • 19
    • 22544460537 scopus 로고    scopus 로고
    • Crystal structure of bacteriophage lambda cII and its DNA complex
    • Jain D, et al. (2005) Crystal structure of bacteriophage lambda cII and its DNA complex. Mol Cell 19(2):259-269.
    • (2005) Mol Cell , vol.19 , Issue.2 , pp. 259-269
    • Jain, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.