메뉴 건너뛰기




Volumn 19, Issue 3, 2005, Pages 398-401

Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin

Author keywords

Fosfomycin; Haemophilus influenzae; MurA; MurZ; UDP N Acetylglucosamine; UDP N Acetylglucosamine Enolpyruvyl Transferase

Indexed keywords

FOSFOMYCIN; TRANSFERASE; UDP N ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; UDP N ACETYLGLUCOSAMINE 1 CARBOXYVINYLTRANSFERASE; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE;

EID: 27244449189     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (13)
  • 1
    • 0034770091 scopus 로고    scopus 로고
    • Identification and characterization of new inhibitors of the Escherichia coli MurA enzyme
    • Baum, E. Z., Montenegro, D. A., Licata, L., Turchi, I., Webb, G. C., et al. (2001) Identification and characterization of new inhibitors of the Escherichia coli MurA enzyme. Antimicrob. Agents Chemother. 45, 3182-3188.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3182-3188
    • Baum, E.Z.1    Montenegro, D.A.2    Licata, L.3    Turchi, I.4    Webb, G.C.5
  • 2
    • 0029064598 scopus 로고
    • MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli
    • Brown, E. D., Vivas, E. I., Walsh, C. T., and Kolter, R. (1995) MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J. Bacteriol. 177, 4194-4197.
    • (1995) J. Bacteriol. , vol.177 , pp. 4194-4197
    • Brown, E.D.1    Vivas, E.I.2    Walsh, C.T.3    Kolter, R.4
  • 3
    • 0026880575 scopus 로고
    • Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance
    • Bugg, T. D. and Walsh, C. T. (1992) Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistance. Nat. Prod. Rep. 9, 199-215.
    • (1992) Nat. Prod. Rep. , vol.9 , pp. 199-215
    • Bugg, T.D.1    Walsh, C.T.2
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 5
    • 0033939999 scopus 로고    scopus 로고
    • Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria
    • Du, W., Brown, J. R., Sylvester, D. R., Huang, J., Chalker, A. F., et al. (2000) Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria. J. Bacteriol. 182, 4146-4152.
    • (2000) J. Bacteriol. , vol.182 , pp. 4146-4152
    • Du, W.1    Brown, J.R.2    Sylvester, D.R.3    Huang, J.4    Chalker, A.F.5
  • 6
    • 0034257036 scopus 로고    scopus 로고
    • Comparative X-ray analysis of the un-liganded fosfomycin-target murA
    • Eschenburg, S. and Schönbrunn, E. (2000) Comparative X-ray analysis of the un-liganded fosfomycin-target murA. Proteins 40, 290-298.
    • (2000) Proteins , vol.40 , pp. 290-298
    • Eschenburg, S.1    Schönbrunn, E.2
  • 7
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R. D., Adams, M. D., White, O., Clayton, R. A., Kirkness, E. F., et al. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1    Adams, M.D.2    White, O.3    Clayton, R.A.4    Kirkness, E.F.5
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-493.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-493
    • Matthews, B.W.1
  • 12
    • 0030587522 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
    • Schönbrunn, E., Sack, S., Eschenburg, S., Perrakis, A., Krekel, F., et al. (1996) Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure 4, 1065-1075.
    • (1996) Structure , vol.4 , pp. 1065-1075
    • Schönbrunn, E.1    Sack, S.2    Eschenburg, S.3    Perrakis, A.4    Krekel, F.5
  • 13
    • 0030589610 scopus 로고    scopus 로고
    • Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin
    • Skarzynski, T., Mistry, A., Wonacott, A., Hutchinson, S. E., Kelly, V. A., et al. (1996) Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure 4, 1465-1474.
    • (1996) Structure , vol.4 , pp. 1465-1474
    • Skarzynski, T.1    Mistry, A.2    Wonacott, A.3    Hutchinson, S.E.4    Kelly, V.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.