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Volumn 9, Issue 6, 2000, Pages 1045-1052

The 1.9 Å crystal structure of Escherichia coli MurG, a membrane- associated glycosyltransferase involved in peptidoglycan biosynthesis

Author keywords

Glycosyltransferase; MurG; Peptidoglycan biosynthesis; X ray crystal structure

Indexed keywords

BACTERIAL ENZYME; GLYCOSYLTRANSFERASE; PEPTIDOGLYCAN; N ACETYLGLUCOSAMINYLTRANSFERASE; OUTER MEMBRANE PROTEIN; UDP N ACETYLGLUCOSAMINE N ACETYLMURAMYL (PENTAPEPTIDE)PYROPHOSPHORYL UNDECAPRENOL N ACETYLGLUCOSAMINE TRANSFERASE; UDP-N-ACETYLGLUCOSAMINE-N-ACETYLMURAMYL-(PENTAPEPTIDE)PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE;

EID: 0033623762     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.6.1045     Document Type: Article
Times cited : (236)

References (27)
  • 1
    • 0026685776 scopus 로고
    • Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold: Implications for nucleotide specificity
    • Baker PJ, Britton KL, Rice DW, Rob A, Stillman TJ. 1492. Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold: Implications for nucleotide specificity. J Mol Biol 228:662-671.
    • (1492) J Mol Biol , vol.228 , pp. 662-671
    • Baker, P.J.1    Britton, K.L.2    Rice, D.W.3    Rob, A.4    Stillman, T.J.5
  • 2
    • 0029056202 scopus 로고
    • An enzyme-substrate complex involved in bacterial cell wall biosynthesis
    • Benson TE, Filman DJ, Walsh CT, Hogle JM. 1995. An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat Struct Biol 2:644-653.
    • (1995) Nat Struct Biol , vol.2 , pp. 644-653
    • Benson, T.E.1    Filman, D.J.2    Walsh, C.T.3    Hogle, J.M.4
  • 6
    • 0026880575 scopus 로고
    • Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance
    • Bugg TDH, Walsh CT. 1992. Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance. Nat Prod Rep 199-215.
    • (1992) Nat Prod Rep , pp. 199-215
    • Bugg, T.D.H.1    Walsh, C.T.2
  • 7
    • 0027405768 scopus 로고
    • The final step of peptidoglycan subunit assembly m Escherichia coli occurs in the cytoplasm
    • Bupp K, van Heijenoort J. 1993. The final step of peptidoglycan subunit assembly m Escherichia coli occurs in the cytoplasm. J Bacteriol 175:1841-1843.
    • (1993) J Bacteriol , vol.175 , pp. 1841-1843
    • Bupp, K.1    Van Heijenoort, J.2
  • 8
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. 1: Conserved stereochemistry of cofactor binding
    • Carugo O, Argos P. 1997. NADP-dependent enzymes. 1: Conserved stereochemistry of cofactor binding. Proteins 28:10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computing Project Number 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 10
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho sugar transferase. SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • Charnok SJ, Davies GJ. 1999. Structure of the nucleotide-diphospho sugar transferase. SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38:6380-6385.
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnok, S.J.1    Davies, G.J.2
  • 12
    • 0028151598 scopus 로고
    • Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3A resolution
    • Fan C, Moews PC, Walsh CT, Knox JR. 1994. Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3A resolution. Science 266:439-443.
    • (1994) Science , vol.266 , pp. 439-443
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 13
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4 galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel LN, Cambillau C, Bourne Y. 1999. Crystal structures of the bovine β4 galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J 18:3546-3557.
    • (1999) EMBO J , vol.18 , pp. 3546-3557
    • Gastinel, L.N.1    Cambillau, C.2    Bourne, Y.3
  • 14
    • 0033595530 scopus 로고    scopus 로고
    • The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues
    • Ha S, Chang E, Lo M-C, Men H, Park P, Ge M, Walker S. 1999. The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues. J Am Chem Soc 121:8415-8426.
    • (1999) J Am Chem Soc , vol.121 , pp. 8415-8426
    • Ha, S.1    Chang, E.2    Lo, M.-C.3    Men, H.4    Park, P.5    Ge, M.6    Walker, S.7
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0032844594 scopus 로고    scopus 로고
    • Conserved domains of glycosyltransferases
    • Kapitonov D, Yu RK. 1999. Conserved domains of glycosyltransferases. Glycobiology 9:961-978.
    • (1999) Glycobiology , vol.9 , pp. 961-978
    • Kapitonov, D.1    Yu, R.K.2
  • 17
    • 0032787505 scopus 로고    scopus 로고
    • Overexpression of core 2 N-acetylglycosaminyltransferase enhances cytokine actions and induces hypertrophic myocardium in transgenic mice
    • Koya D, Dennis JW, Warren CE, Takahara N, Schoen FJ, Nishio Y, Nakajima T, Lipes MA, King GL. 1999. Overexpression of core 2 N-acetylglycosaminyltransferase enhances cytokine actions and induces hypertrophic myocardium in transgenic mice. FASEB J 13:2329-2337.
    • (1999) FASEB J , vol.13 , pp. 2329-2337
    • Koya, D.1    Dennis, J.W.2    Warren, C.E.3    Takahara, N.4    Schoen, F.J.5    Nishio, Y.6    Nakajima, T.7    Lipes, M.A.8    King, G.L.9
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0032542717 scopus 로고    scopus 로고
    • Substrate synthesis and activity assay for MurG
    • Men H, Park P, Ge M, Walker S. 1998. Substrate synthesis and activity assay for MurG. J Am Chem Soc 120:2484-2485.
    • (1998) J Am Chem Soc , vol.120 , pp. 2484-2485
    • Men, H.1    Park, P.2    Ge, M.3    Walker, S.4
  • 21
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merrit EA, Murphy ME. 1994. Raster3D Version 2.0: A program for photorealistic molecular graphics. Acta Crystallogr D 50:869-873.
    • (1994) Acta Crystallogr D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.2
  • 22
    • 0345588683 scopus 로고    scopus 로고
    • T4 phage β-glucosyltransferase: Substrate binding and proposed catalytic mechanism
    • Moréra S, Imberty A, Aschke-Sonnenborn U, Rüger W, Freemont PS. 1999. T4 phage β-glucosyltransferase: Substrate binding and proposed catalytic mechanism. J Mol Biol 292:717-730.
    • (1999) J Mol Biol , vol.292 , pp. 717-730
    • Moréra, S.1    Imberty, A.2    Aschke-Sonnenborn, U.3    Rüger, W.4    Freemont, P.S.5
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon E, Bertozzi CR. 2000. Cell surface engineering by a modified Staudinger reaction. Science 287:2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 25
    • 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 SE, Kelly VA, Duncan K. 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    Duncan, K.6
  • 26
    • 0032712592 scopus 로고    scopus 로고
    • Trafficking of oligomannosides released during N-glycosylation: A clearing mechanism of the rough endoplasmic reticulum
    • Verbert A, Cacan R. 1999. Trafficking of oligomannosides released during N-glycosylation: A clearing mechanism of the rough endoplasmic reticulum. Biochim Biophys Acta 1473:137-146.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 137-146
    • Verbert, A.1    Cacan, R.2
  • 27
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink A, Rüger W, Driessen HPC, Freemont PS. 1994. Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J 13:3413-3422.
    • (1994) EMBO J , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Rüger, W.2    Driessen, H.P.C.3    Freemont, P.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.