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Volumn 51, Issue 45, 2012, Pages 9164-9177

On the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BINARY COMPLEXES; CATALYTIC ACIDS; CELL WALLS; CHAIR CONFORMATIONS; CONFORMATIONAL STATE; GLYCOPEPTIDES; GLYCOSIDIC BOND; GLYCOSIDIC BOND CLEAVAGE; N-ACETYLGLUCOSAMINE; N-ACETYLMURAMIC ACID; PEPTIDOGLYCANS; PRECISE MODELING; PREFERENTIAL BINDING; SITE DIRECTED MUTAGENESIS; SUBSITES; SUBSTRATE-BOUND; SUBSTRATE-FREE; SUGAR RINGS; TERNARY COMPLEX;

EID: 84869078754     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300900t     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 0029692069 scopus 로고    scopus 로고
    • Lytic transglycosylases
    • Höltje, J. V. (1996) Lytic transglycosylases EXS 75, 425-429
    • (1996) EXS , vol.75 , pp. 425-429
    • Höltje, J.V.1
  • 2
  • 3
    • 84455162073 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Escherichia coli
    • van Heijenoort, J. (2011) Peptidoglycan hydrolases of Escherichia coli Microbiol. Mol. Biol. Rev. 75, 636-663
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 636-663
    • Van Heijenoort, J.1
  • 4
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn, N. T. and Clarke, A. J. (2001) Identification of four families of peptidoglycan lytic transglycosylases J. Mol. Evol. 52, 78-84
    • (2001) J. Mol. Evol. , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 6
    • 0029739727 scopus 로고    scopus 로고
    • Identification of new members of the lytic transglycosylase family in Haemophilus influenzae and Escherichia coli
    • Dijkstra, A. J. and Keck, W. (1996) Identification of new members of the lytic transglycosylase family in Haemophilus influenzae and Escherichia coli Microb. Drug Resist. 2, 141-145
    • (1996) Microb. Drug Resist. , vol.2 , pp. 141-145
    • Dijkstra, A.J.1    Keck, W.2
  • 7
    • 0031748682 scopus 로고    scopus 로고
    • Membrane-bound lytic endotransglycosylase in Escherichia coli
    • Kraft, A. R., Templin, M. F., and Höltje, J. V. (1998) Membrane-bound lytic endotransglycosylase in Escherichia coli J. Bacteriol. 180, 3441-3447
    • (1998) J. Bacteriol. , vol.180 , pp. 3441-3447
    • Kraft, A.R.1    Templin, M.F.2    Höltje, J.V.3
  • 8
    • 24944507285 scopus 로고    scopus 로고
    • Crystal structure of MltA from reveals a unique lytic transglycosylase fold
    • van Straaten, K. E., Dijkstra, B. W., Vollmer, W., and Thunnissen, A. M. W. H. (2005) Crystal structure of MltA from reveals a unique lytic transglycosylase fold J. Mol. Biol. 352, 1068-1080
    • (2005) J. Mol. Biol. , vol.352 , pp. 1068-1080
    • Van Straaten, K.E.1    Dijkstra, B.W.2    Vollmer, W.3    Thunnissen, A.M.W.H.4
  • 9
    • 34547138663 scopus 로고    scopus 로고
    • Structure of Escherichia coli lytic transglycosylase MltA with bound chitohexaose: Implications for peptidoglycan binding and cleavage
    • van Straaten, K. E., Barends, T. R., Dijkstra, B. W., and Thunnissen, A. M. W. H. (2007) Structure of Escherichia coli lytic transglycosylase MltA with bound chitohexaose: Implications for peptidoglycan binding and cleavage J. Biol. Chem. 282, 21197-21205
    • (2007) J. Biol. Chem. , vol.282 , pp. 21197-21205
    • Van Straaten, K.E.1    Barends, T.R.2    Dijkstra, B.W.3    Thunnissen, A.M.W.H.4
  • 10
    • 0342901668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand
    • van Asselt, E. J., Dijkstra, A. J., Kalk, K. H., Takacs, B., Keck, W., and Dijkstra, B. W. (1999) Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand Structure 7, 1167-1180
    • (1999) Structure , vol.7 , pp. 1167-1180
    • Van Asselt, E.J.1    Dijkstra, A.J.2    Kalk, K.H.3    Takacs, B.4    Keck, W.5    Dijkstra, B.W.6
  • 11
    • 51749085075 scopus 로고    scopus 로고
    • Lytic transglycosylase MltB of Escherichia coli and its role in recycling of peptidoglycan strands of bacterial cell wall
    • Suvorov, M., Lee, M., Hesek, D., Boggess, B., and Mobashery, S. (2008) Lytic transglycosylase MltB of Escherichia coli and its role in recycling of peptidoglycan strands of bacterial cell wall J. Am. Chem. Soc. 130, 11878-11879
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11878-11879
    • Suvorov, M.1    Lee, M.2    Hesek, D.3    Boggess, B.4    Mobashery, S.5
  • 12
    • 43749112959 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase
    • Scheurwater, E. M. and Clarke, A. J. (2008) The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase J. Biol. Chem. 283, 8363-8373
    • (2008) J. Biol. Chem. , vol.283 , pp. 8363-8373
    • Scheurwater, E.M.1    Clarke, A.J.2
  • 13
    • 77951990234 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction analysis of the lytic transglycosylase MltF from Escherichia coli
    • Madoori, P. K. and Thunnissen, A. M. W. H. (2010) Purification, crystallization and preliminary X-ray diffraction analysis of the lytic transglycosylase MltF from Escherichia coli Acta Crystallogr. F66, 534-538
    • (2010) Acta Crystallogr. , vol.66 , pp. 534-538
    • Madoori, P.K.1    Thunnissen, A.M.W.H.2
  • 14
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • Thunnissen, A. M. W. H., Isaacs, N. W., and Dijkstra, B. W. (1995) The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes Proteins 22, 245-258
    • (1995) Proteins , vol.22 , pp. 245-258
    • Thunnissen, A.M.W.H.1    Isaacs, N.W.2    Dijkstra, B.W.3
  • 15
    • 0028874610 scopus 로고
    • Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A: Implications for the enzymatic mechanism
    • Thunnissen, A. M. W. H., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1995) Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A: Implications for the enzymatic mechanism Biochemistry 34, 12729-12737
    • (1995) Biochemistry , vol.34 , pp. 12729-12737
    • Thunnissen, A.M.W.H.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 16
    • 0033609769 scopus 로고    scopus 로고
    • High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment
    • van Asselt, E. J., Thunnissen, A. M. W. H., and Dijkstra, B. W. (1999) High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment J. Mol. Biol. 291, 877-898
    • (1999) J. Mol. Biol. , vol.291 , pp. 877-898
    • Van Asselt, E.J.1    Thunnissen, A.M.W.H.2    Dijkstra, B.W.3
  • 17
    • 0034728363 scopus 로고    scopus 로고
    • Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan
    • van Asselt, E. J., Kalk, K. H., and Dijkstra, B. W. (2000) Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan Biochemistry 39, 1924-1934
    • (2000) Biochemistry , vol.39 , pp. 1924-1934
    • Van Asselt, E.J.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 18
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies, G. J., Wilson, K. S., and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321 (Pt 2) 557-559
    • (1997) Biochem. J. , vol.321 , Issue.PART 2 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 19
  • 20
    • 34948837924 scopus 로고    scopus 로고
    • Role of Ser216 in the mechanism of action of membrane-bound lytic transglycosylase B: Further evidence for substrate-assisted catalysis
    • Reid, C. W., Legaree, B. A., and Clarke, A. J. (2007) Role of Ser216 in the mechanism of action of membrane-bound lytic transglycosylase B: Further evidence for substrate-assisted catalysis FEBS Lett. 581, 4988-4992
    • (2007) FEBS Lett. , vol.581 , pp. 4988-4992
    • Reid, C.W.1    Legaree, B.A.2    Clarke, A.J.3
  • 22
    • 0026668027 scopus 로고
    • A murein hydrolase is the specific target of bulgecin in Escherichia coli
    • Templin, M. F., Edwards, D. H., and Holtje, J. V. (1992) A murein hydrolase is the specific target of bulgecin in Escherichia coli J. Biol. Chem. 267, 20039-20043
    • (1992) J. Biol. Chem. , vol.267 , pp. 20039-20043
    • Templin, M.F.1    Edwards, D.H.2    Holtje, J.V.3
  • 23
    • 34548319070 scopus 로고    scopus 로고
    • High-throughput cloning and expression in recalcitrant bacteria
    • Geertsma, E. R. and Poolman, B. (2007) High-throughput cloning and expression in recalcitrant bacteria Nat. Methods 4, 705-707
    • (2007) Nat. Methods , vol.4 , pp. 705-707
    • Geertsma, E.R.1    Poolman, B.2
  • 24
    • 0014060395 scopus 로고
    • Measurement of bacteriolytic enzymes
    • Hash, J. H. (1967) Measurement of bacteriolytic enzymes J. Bacteriol. 93, 1201-1202
    • (1967) J. Bacteriol. , vol.93 , pp. 1201-1202
    • Hash, J.H.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 ()
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 27
    • 0033082065 scopus 로고    scopus 로고
    • Optimizing shake-and-bake for proteins
    • Weeks, C. M. and Miller, R. (1999) Optimizing shake-and-bake for proteins Acta Crystallogr. D55, 492-500
    • (1999) Acta Crystallogr. , vol.55 , pp. 492-500
    • Weeks, C.M.1    Miller, R.2
  • 28
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M., and Paciorek, W. (2003) Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0 Acta Crystallogr. D59, 2023-2030
    • (2003) Acta Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 29
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J. P. and Leslie, A. G. (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase Acta Crystallogr. D52, 30-42
    • (1996) Acta Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 31
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brünger, A. T. (2007) Version 1.2 of the crystallography and NMR system Nat. Protoc. 2, 2728-2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brünger, A.T.1
  • 32
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26, 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 33
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP
    • Vagin, A. and Teplyakov, A. (2010) Molecular replacement with MOLREP Acta Crystallogr. D66, 22-25
    • (2010) Acta Crystallogr. , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive python-based system for macromolecular structure solution
    • Adams, P. D., Afonine, P. V., Bunkoczi, G., Chen, V. B., and Davis, I. W. 2010, PHENIX: A comprehensive python-based system for macromolecular structure solution Acta Crystallogr. D66, 213-221
    • (2010) Acta Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkoczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 37
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D57, 122-133
    • (2001) Acta Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 39
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • Poirot, O., O'Toole, E., and Notredame, C. (2003) Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments Nucleic Acids Res. 31, 3503-3506
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 40
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D60, 2256-2268
    • (2004) Acta Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 41
    • 84874756729 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system, version 1.5.0.1.
    • Schrödinger, L. (2012) The PyMOL molecular graphics system, version 1.5.0.1.
    • (2012)
    • Schrödinger, L.1
  • 42
    • 84855363564 scopus 로고    scopus 로고
    • Regulation of biofilm components in Salmonella enterica serovar typhimurium by lytic transglycosylases involved in cell wall turnover
    • Monteiro, C., Fang, X., Ahmad, I., Gomelsky, M., and Römling, U. (2011) Regulation of biofilm components in Salmonella enterica serovar typhimurium by lytic transglycosylases involved in cell wall turnover J. Bacteriol. 193, 6443-6451
    • (2011) J. Bacteriol. , vol.193 , pp. 6443-6451
    • Monteiro, C.1    Fang, X.2    Ahmad, I.3    Gomelsky, M.4    Römling, U.5


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