메뉴 건너뛰기




Volumn 20, Issue 9, 2013, Pages 1002-1008

Crystal structure of the Pseudomonas aeruginosa MurG: UDP-GlcNAc substrate complex

Author keywords

Enzymology; Fluorimetry; Peptidoglycan biosynthesis; Transferase; X ray crystallography

Indexed keywords

GLUCOSYLTRANSFERASE; LIPID; LIPID 1; PROTEIN MURG; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 84882350101     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511320090006     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 0037326937 scopus 로고    scopus 로고
    • Multicentre surveillance of pseudomonas aeruginosa susceptibility patterns in nosocomial infections
    • van Eldere J. Multicentre surveillance of Pseudomonas aeruginosa susceptibility patterns in nosocomial infections. J. Antimicrob. Chemother., 2003, 51, 347-52.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 347-352
    • Van Eldere, J.1
  • 2
    • 1642422948 scopus 로고    scopus 로고
    • Efflux-mediated multiresistance in gram-negative bacteria
    • Poole K Efflux-mediated multiresistance in Gram-negative bacteria. Clin. Microbiol. Infect., 2004, 10, 12-26.
    • (2004) Clin. Microbiol. Infect. , vol.10 , pp. 12-26
    • Poole, K.1
  • 3
    • 77955434167 scopus 로고
    • Pseudomonas aeruginosa: Infections and treatment
    • Balcht AL, Smith RP Pseudomonas Aeruginosa: Infections and Treatment. Informa. Health Care, 1994, pp 83-84.
    • (1994) Informa. Health Care , pp. 83-84
    • Balcht, A.L.1    Smith, R.P.2
  • 4
    • 0036431716 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa in cystic fibrosis: Pathogenesis and persistence
    • Davies JC Pseudomonas aeruginosa in cystic fibrosis: pathogenesis and persistence. Paediatr. Respir. Rev., 2002, 3, 128-34.
    • (2002) Paediatr. Respir. Rev. , vol.3 , pp. 128-134
    • Davies, J.C.1
  • 6
    • 0036733378 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa: Resistance and therapy
    • Cunha BA Pseudomonas aeruginosa: resistance and therapy. Semin. Respir. Infect., 2002, 17, 231-9.
    • (2002) Semin. Respir. Infect. , vol.17 , pp. 231-239
    • Cunha, B.A.1
  • 7
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt BG Resistance to antibiotics mediated by target alterations. Science, 1994, 264, 388-93.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 8
    • 0037241238 scopus 로고    scopus 로고
    • Structure-based design approaches to cell wall biosynthesis inhibitors
    • Katz AH, Caufield CE. Structure-based design approaches to cell wall biosynthesis inhibitors. Curr. Pharm. Des., 2003, 9, 857-866.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 857-866
    • Katz, A.H.1    Caufield, C.E.2
  • 9
    • 0037223505 scopus 로고    scopus 로고
    • Structure and function of the mur enzymes: Development of novel inhibitors
    • El Zoeiby A, Sanschagrin F, Levesque RC Structure and function of the Mur enzymes: development of novel inhibitors. Mol. Microbiol., 2003, 47, 1-12.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1-12
    • El Zoeiby, A.1    Sanschagrin, F.2    Levesque, R.C.3
  • 10
    • 0026880575 scopus 로고
    • Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance
    • Bugg TDH, Walsh CT Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance. Nat. Prod. Rep., 1992, 199-215.
    • (1992) Nat. Prod. Rep. , pp. 199-215
    • Bugg, T.D.H.1    Walsh, C.T.2
  • 11
    • 61549097473 scopus 로고    scopus 로고
    • Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes murd and murf by structure-based virtual screening
    • Turk S, Kovac A, Boniface A, Bostock JM, Chopra I, Blanot D, Gobec S. Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening. Bioorg. Med. Chem., 2009, 17, 1884-9.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1884-1889
    • Turk, S.1    Kovac, A.2    Boniface, A.3    Bostock, J.M.4    Chopra, I.5    Blanot, D.6    Gobec, S.7
  • 12
    • 34548258863 scopus 로고    scopus 로고
    • Prezelj a development of novel inhibitors targeting intracellular steps of peptidoglycan biosynthesis
    • Kotnik M, Anderluh PS, Prezelj A Development of novel inhibitors targeting intracellular steps of peptidoglycan biosynthesis. Curr. Pharm. Des., 2007, 13, 2283-309.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2283-2309
    • Kotnik, M.1    Anderluh, P.S.2
  • 13
    • 33644558385 scopus 로고    scopus 로고
    • Does the cell wall of bacteria remain a viable source of targets for novel antibiotics?
    • Silver LL Does the cell wall of bacteria remain a viable source of targets for novel antibiotics? Biochem. Pharmacol., 2006, 71, 996-1005.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 996-1005
    • Silver, L.L.1
  • 14
    • 33947132188 scopus 로고    scopus 로고
    • Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis
    • Lovering A, de Castro L, Lim D, Strynadka N Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science, 2007, 315, 1402-5.
    • (2007) Science , vol.315 , pp. 1402-1405
    • Lovering, A.1    De Castro, L.2    Lim, D.3    Strynadka, N.4
  • 15
    • 0032542717 scopus 로고    scopus 로고
    • Substrate synthesis and activity assay for murg
    • Men H, Park P, Ge M, Walker S Substrate Synthesis and Activity Assay for MurG. J. Am. Chem. Soc., 1998, 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
  • 16
    • 77950026621 scopus 로고    scopus 로고
    • Inhibition of escherichia coli glycosyltransferase murg and mycobacterium tuberculosis gal transferase by uridine-linked transition state mimics
    • Trunkfield AE, Gurcha SS, Besra GS, Bugg TD Inhibition of Escherichia coli glycosyltransferase MurG and Mycobacterium tuberculosis Gal transferase by uridine-linked transition state mimics. Bioorg. Med. Chem., 2010, 18, 2651-63.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2651-2663
    • Trunkfield, A.E.1    Gurcha, S.S.2    Besra, G.S.3    Bugg, T.D.4
  • 17
    • 0019120833 scopus 로고
    • Identification of new genes in a cell envelope-cell division gene cluster of escherichia coli: Cell envelope gene murg
    • Salmond GPC, Lutkenhaus JF, Donachie WD Identification of new genes in a cell envelope-cell division gene cluster of Escherichia coli: cell envelope gene MurG. J. Bacteriol., 1980, 144, 438-440.
    • (1980) J. Bacteriol. , vol.144 , pp. 438-440
    • Salmond, G.P.C.1    Lutkenhaus, J.F.2    Donachie, W.D.3
  • 18
    • 0025833399 scopus 로고
    • The murg gene of escherichia coli codes for the udp-nacetylglucosamine: N.-Acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol nacetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis
    • Mengin-Lecreulx D, Texier L, Rousseau M, van Heijenoort J The murG gene of Escherichia coli codes for the UDP.-Nacetylglucosamine: N.-Acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol Nacetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis. J. Bacteriol., 1991, 173, 4625-36.
    • (1991) J. Bacteriol. , vol.173 , pp. 4625-4636
    • Mengin-Lecreulx, D.1    Texier, L.2    Rousseau, M.3    Van Heijenoort, J.4
  • 21
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 a crystal structure of escherichia coli murg, a membrane-Associated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha S, Walker D, Shi Y, Walker S The 1.9 A crystal structure of Escherichia coli MurG, a membrane-Associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci., 2000, 9, 1045-52.
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 29
    • 0042357149 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. The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues. J. Am. Chem. Soc., 1999, 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
  • 30
    • 0037188393 scopus 로고    scopus 로고
    • Intrinsic lipid preferences and kinetic mechanism of escherichia coli murg
    • Chen L, Men H, Ha S, Ye X.-Y, Brunner L, Hu Y, Walker S Intrinsic Lipid Preferences and Kinetic Mechanism of Escherichia coli MurG. Biochemistry, 2002, 41, 6824-6833.
    • (2002) Biochemistry , vol.41 , pp. 6824-6833
    • Chen, L.1    Men, H.2    Ha, S.3    Ye, X.-Y.4    Brunner, L.5    Hu, Y.6    Walker, S.7
  • 31
    • 0030893657 scopus 로고    scopus 로고
    • Nadp-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo O, Argos P. NADP.-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins, 1997, 28, 10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 32
    • 13444307044 scopus 로고    scopus 로고
    • Henrick k secondary-structure matching (ssm), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Cryst. D Biol. Crystallogr., 2004, 60, 2256-2268.
    • (2004) Acta Cryst. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1
  • 33
    • 36249031916 scopus 로고    scopus 로고
    • Role of the amino acid invariants in the active site of murg as evaluated by site-direct mutagenesis
    • Crouvoisier M, Auger G, Blanot D, Mengin-Lecreulx D Role of the amino acid invariants in the active site of MurG as evaluated by site-direct mutagenesis. Biochemie, 2007, 89, 1498-1508.
    • (2007) Biochemie , vol.89 , pp. 1498-1508
    • Crouvoisier, M.1    Auger, G.2    Blanot, D.3    Mengin-Lecreulx, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.