메뉴 건너뛰기




Volumn 20, Issue 12, 2012, Pages 2103-2115

Targeting the cell wall of mycobacterium tuberculosis: Structure and mechanism of L,D-transpeptidase 2

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; CARBAPENEM; CYSTEINE; ERTAPENEM; IMIPENEM; L,D TRANSPEPTIDASE 2; MEROPENEM; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 84870500858     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.09.016     Document Type: Article
Times cited : (94)

References (39)
  • 1
    • 0018654090 scopus 로고
    • Three-dimensional structure of immunoglobulins
    • L.M. Amzel, and R.J. Poljak Three-dimensional structure of immunoglobulins Annu. Rev. Biochem. 48 1979 961 997
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 961-997
    • Amzel, L.M.1    Poljak, R.J.2
  • 3
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • A. Bateman, and M. Bycroft The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD) J. Mol. Biol. 299 2000 1113 1119
    • (2000) J. Mol. Biol. , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 4
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • J.C. Betts, P.T. Lukey, L.C. Robb, R.A. McAdam, and K. Duncan Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling Mol. Microbiol. 43 2002 717 731
    • (2002) Mol. Microbiol. , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 6
    • 30344465753 scopus 로고    scopus 로고
    • B. subtilis ykuD protein at 2.0 A resolution: Insights into the structure and function of a novel, ubiquitous family of bacterial enzymes
    • J. Bielnicki, Y. Devedjiev, U. Derewenda, Z. Dauter, A. Joachimiak, and Z.S. Derewenda B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes Proteins 62 2006 144 151
    • (2006) Proteins , vol.62 , pp. 144-151
    • Bielnicki, J.1    Devedjiev, Y.2    Derewenda, U.3    Dauter, Z.4    Joachimiak, A.5    Derewenda, Z.S.6
  • 7
    • 0034679958 scopus 로고    scopus 로고
    • Lipid lunch for persistent pathogen
    • W. Bishai Lipid lunch for persistent pathogen Nature 406 2000 683 685
    • (2000) Nature , vol.406 , pp. 683-685
    • Bishai, W.1
  • 9
    • 80053614751 scopus 로고    scopus 로고
    • Distinct pathways for modification of the bacterial cell wall by non-canonical D-amino acids
    • F. Cava, M.A. de Pedro, H. Lam, B.M. Davis, and M.K. Waldor Distinct pathways for modification of the bacterial cell wall by non-canonical D-amino acids EMBO J. 30 2011 3442 3453
    • (2011) EMBO J , vol.30 , pp. 3442-3453
    • Cava, F.1    De Pedro, M.A.2    Lam, H.3    Davis, B.M.4    Waldor, M.K.5
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 11
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • G. Dodson, and A. Wlodawer Catalytic triads and their relatives Trends Biochem. Sci. 23 1998 347 352
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 14
    • 43949084039 scopus 로고    scopus 로고
    • Multidrug-resistant and extensively drug-resistant tuberculosis: The National Institute of Allergy and Infectious Diseases Research agenda and recommendations for priority research
    • NIAID Tuberculosis Working Group
    • A.S. Fauci NIAID Tuberculosis Working Group Multidrug-resistant and extensively drug-resistant tuberculosis: the National Institute of Allergy and Infectious Diseases Research agenda and recommendations for priority research J. Infect. Dis. 197 2008 1493 1498
    • (2008) J. Infect. Dis. , vol.197 , pp. 1493-1498
    • Fauci, A.S.1
  • 15
    • 0036898699 scopus 로고    scopus 로고
    • Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent
    • C. Goffin, and J.M. Ghuysen Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent Microbiol. Mol. Biol. Rev. 66 2002 702 738
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 702-738
    • Goffin, C.1    Ghuysen, J.M.2
  • 16
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • R. Gupta, M. Lavollay, J.L. Mainardi, M. Arthur, W.R. Bishai, and G. Lamichhane The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin Nat. Med. 16 2010 466 469
    • (2010) Nat. Med. , vol.16 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5    Lamichhane, G.6
  • 17
    • 61349183785 scopus 로고    scopus 로고
    • Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis
    • J.E. Hugonnet, L.W. Tremblay, H.I. Boshoff, C.E. Barry 3rd, and J.S. Blanchard Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis Science 323 2009 1215 1218
    • (2009) Science , vol.323 , pp. 1215-1218
    • Hugonnet, J.E.1    Tremblay, L.W.2    Boshoff, H.I.3    Barry III, C.E.4    Blanchard, J.S.5
  • 18
    • 0038628994 scopus 로고    scopus 로고
    • Bactericidal and sterilizing activities of antituberculosis drugs during the first 14 days
    • A. Jindani, C.J. Doré, and D.A. Mitchison Bactericidal and sterilizing activities of antituberculosis drugs during the first 14 days Am. J. Respir. Crit. Care Med. 167 2003 1348 1354
    • (2003) Am. J. Respir. Crit. Care Med. , vol.167 , pp. 1348-1354
    • Jindani, A.1    Doré, C.J.2    Mitchison, D.A.3
  • 19
    • 84855195248 scopus 로고    scopus 로고
    • Characterization and transcriptome analysis of Mycobacterium tuberculosis persisters
    • I. Keren, S. Minami, E. Rubin, and K. Lewis Characterization and transcriptome analysis of Mycobacterium tuberculosis persisters MBio 2 2011 e00100 e00111
    • (2011) MBio , vol.2
    • Keren, I.1    Minami, S.2    Rubin, E.3    Lewis, K.4
  • 20
    • 79953734276 scopus 로고    scopus 로고
    • Macromolecular complexes in crystals and solutions
    • E. Krissinel Macromolecular complexes in crystals and solutions Acta Crystallogr. D Biol. Crystallogr. 67 2011 376 385
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 376-385
    • Krissinel, E.1
  • 21
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation
    • M. Lavollay, M. Arthur, M. Fourgeaud, L. Dubost, A. Marie, N. Veziris, D. Blanot, L. Gutmann, and J.L. Mainardi The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation J. Bacteriol. 190 2008 4360 4366
    • (2008) J. Bacteriol. , vol.190 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5    Veziris, N.6    Blanot, D.7    Gutmann, L.8    Mainardi, J.L.9
  • 23
    • 33845607284 scopus 로고    scopus 로고
    • Persister cells, dormancy and infectious disease
    • K. Lewis Persister cells, dormancy and infectious disease Nat. Rev. Microbiol. 5 2007 48 56
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 48-56
    • Lewis, K.1
  • 26
    • 0013943408 scopus 로고
    • Biosynthesis in the bacterial cell wall
    • M. Matsuhashi [Biosynthesis in the bacterial cell wall] Tanpakushitsu Kakusan Koso 11 1966 875 886
    • (1966) Tanpakushitsu Kakusan Koso , vol.11 , pp. 875-886
    • Matsuhashi, M.1
  • 27
    • 0000891757 scopus 로고    scopus 로고
    • Diagnosis and treatment of disease caused by nontuberculous mycobacteria. This official statement of the American Thoracic Society was approved by the Board of Directors, March 1997. Medical Section of the American Lung Association
    • Medical Section of the American Lung Association
    • Medical Section of the American Lung Association Diagnosis and treatment of disease caused by nontuberculous mycobacteria. This official statement of the American Thoracic Society was approved by the Board of Directors, March 1997. Medical Section of the American Lung Association Am. J. Respir. Crit. Care Med. 156 1997 S1 S25
    • (1997) Am. J. Respir. Crit. Care Med. , vol.156
  • 28
    • 0023765072 scopus 로고
    • Imipenem as substrate and inhibitor of beta-lactamases
    • J. Monks, and S.G. Waley Imipenem as substrate and inhibitor of beta-lactamases Biochem. J. 253 1988 323 328
    • (1988) Biochem. J. , vol.253 , pp. 323-328
    • Monks, J.1    Waley, S.G.2
  • 30
    • 78149446042 scopus 로고    scopus 로고
    • Protective efficacy of BCG overexpressing an L,D-transpeptidase against M. tuberculosis infection
    • S.T. Nolan, and G. Lamichhane Protective efficacy of BCG overexpressing an L,D-transpeptidase against M. tuberculosis infection PLoS One 5 2010 e13773
    • (2010) PLoS One , vol.5 , pp. 13773
    • Nolan, S.T.1    Lamichhane, G.2
  • 31
    • 0015327122 scopus 로고
    • Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate
    • C.H. O'Callaghan, A. Morris, S.M. Kirby, and A.H. Shingler Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate Antimicrob. Agents Chemother. 1 1972 283 288
    • (1972) Antimicrob. Agents Chemother. , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.H.4
  • 32
    • 0023162376 scopus 로고
    • Multiple heavy-atom reagents for macromolecular X-ray structure determination. Application to the nucleosome core particle
    • T.V. O'Halloran, S.J. Lippard, T.J. Richmond, and A. Klug Multiple heavy-atom reagents for macromolecular X-ray structure determination. Application to the nucleosome core particle J. Mol. Biol. 194 1987 705 712
    • (1987) J. Mol. Biol. , vol.194 , pp. 705-712
    • O'Halloran, T.V.1    Lippard, S.J.2    Richmond, T.J.3    Klug, A.4
  • 33
    • 80051695335 scopus 로고    scopus 로고
    • Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links
    • J. Peltier, P. Courtin, I. El Meouche, L. Lemée, M.P. Chapot-Chartier, and J.L. Pons Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links J. Biol. Chem. 286 2011 29053 29062
    • (2011) J. Biol. Chem. , vol.286 , pp. 29053-29062
    • Peltier, J.1    Courtin, P.2    El Meouche, I.3    Lemée, L.4    Chapot-Chartier, M.P.5    Pons, J.L.6
  • 34
    • 0024267619 scopus 로고
    • Amino acid substitutions in structurally related proteins. A pattern recognition approach. Determination of a new and efficient scoring matrix
    • J.L. Risler, M.O. Delorme, H. Delacroix, and A. Henaut Amino acid substitutions in structurally related proteins. A pattern recognition approach. Determination of a new and efficient scoring matrix J. Mol. Biol. 204 1988 1019 1029
    • (1988) J. Mol. Biol. , vol.204 , pp. 1019-1029
    • Risler, J.L.1    Delorme, M.O.2    Delacroix, H.3    Henaut, A.4
  • 36
    • 0023442628 scopus 로고
    • Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli
    • E. Tuomanen, and R. Cozens Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli J. Bacteriol. 169 1987 5308 5310
    • (1987) J. Bacteriol. , vol.169 , pp. 5308-5310
    • Tuomanen, E.1    Cozens, R.2
  • 37
    • 4444220092 scopus 로고    scopus 로고
    • The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)?
    • W. Vollmer, and J.V. Höltje The architecture of the murein (peptidoglycan) in gram-negative bacteria: vertical scaffold or horizontal layer(s)? J. Bacteriol. 186 2004 5978 5987
    • (2004) J. Bacteriol. , vol.186 , pp. 5978-5987
    • Vollmer, W.1    Höltje, J.V.2
  • 39
    • 0016209670 scopus 로고
    • Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria
    • J. Wietzerbin, B.C. Das, J.F. Petit, E. Lederer, M. Leyh-Bouille, and J.M. Ghuysen Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria Biochemistry 13 1974 3471 3476
    • (1974) Biochemistry , vol.13 , pp. 3471-3476
    • Wietzerbin, J.1    Das, B.C.2    Petit, J.F.3    Lederer, E.4    Leyh-Bouille, M.5    Ghuysen, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.