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Volumn 352, Issue 5, 2005, Pages 1068-1080

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

Author keywords

Bacterial cell wall peptidoglycan; Double psi barrel; Glycoside hydrolase; Lytic transglycosylase; X ray crystallography

Indexed keywords

GLYCOSYLTRANSFERASE; HYDROLASE;

EID: 24944507285     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.067     Document Type: Article
Times cited : (50)

References (53)
  • 1
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • J.V. Höltje Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli Microbiol. Mol. Biol. Rev. 62 1998 181 203
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 3
    • 0036843026 scopus 로고    scopus 로고
    • Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli
    • C. Heidrich, A. Ursinus, J. Berger, H. Schwarz, and J.V. Höltje Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli J. Bacteriol. 184 2002 6093 6099
    • (2002) J. Bacteriol. , vol.184 , pp. 6093-6099
    • Heidrich, C.1    Ursinus, A.2    Berger, J.3    Schwarz, H.4    Höltje, J.V.5
  • 4
    • 0028825333 scopus 로고
    • From growth to autolysis: The murein hydrolases in Escherichia coli
    • J.V. Höltje From growth to autolysis: the murein hydrolases in Escherichia coli Arch. Microbiol. 164 1995 243 254
    • (1995) Arch. Microbiol. , vol.164 , pp. 243-254
    • Höltje, J.V.1
  • 5
    • 0031748682 scopus 로고    scopus 로고
    • Membrane-bound lytic endotransglycosylase in Escherichia coli
    • A.R. Kraft, M.F. Templin, and J.V. Höltje Membrane-bound lytic endotransglycosylase in Escherichia coli J. Bacteriol. 180 1998 3441 3447
    • (1998) J. Bacteriol. , vol.180 , pp. 3441-3447
    • Kraft, A.R.1    Templin, M.F.2    Höltje, J.V.3
  • 6
    • 0027240681 scopus 로고
    • Characterization of three different lytic transglycosylases in Escherichia coli
    • T. Romeis, W. Vollmer, and J.V. Holtje Characterization of three different lytic transglycosylases in Escherichia coli FEMS Microbiol. Letters 111 1993 141 146
    • (1993) FEMS Microbiol. Letters , vol.111 , pp. 141-146
    • Romeis, T.1    Vollmer, W.2    Holtje, J.V.3
  • 7
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • N.T. Blackburn, and A.J. Clarke Identification of four families of peptidoglycan lytic transglycosylases J. Mol. Evol. 52 2001 78 84
    • (2001) J. Mol. Evol. , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 9
    • 0026668027 scopus 로고
    • A murein hydrolase is the specific target of bulgecin in Escherichia coli
    • M.F. Templin, D.H. Edwards, and J.V. Höltje A murein hydrolase is the specific target of bulgecin in Escherichia coli J. Biol. Chem. 267 1992 20039 20043
    • (1992) J. Biol. Chem. , vol.267 , pp. 20039-20043
    • Templin, M.F.1    Edwards, D.H.2    Höltje, J.V.3
  • 10
    • 0020403908 scopus 로고
    • Bulgecin, a bacterial metabolite which in concert with beta-lactam antibiotics causes bulge formation
    • A. Imada, K. Kintaka, M. Nakao, and S. Shinagawa Bulgecin, a bacterial metabolite which in concert with beta-lactam antibiotics causes bulge formation J. Antibiot. 35 1982 1400 1403
    • (1982) J. Antibiot. , vol.35 , pp. 1400-1403
    • Imada, A.1    Kintaka, K.2    Nakao, M.3    Shinagawa, S.4
  • 11
    • 0022534924 scopus 로고
    • Novel morphological changes in gram-negative bacteria caused by combination of bulgecin and cefmenoxime
    • M. Nakao, K. Yukishige, M. Kondo, and A. Imada Novel morphological changes in gram-negative bacteria caused by combination of bulgecin and cefmenoxime Antimicrob. Agents Chem. 30 1986 414 417
    • (1986) Antimicrob. Agents Chem. , vol.30 , pp. 414-417
    • Nakao, M.1    Yukishige, K.2    Kondo, M.3    Imada, A.4
  • 13
    • 0033609769 scopus 로고    scopus 로고
    • High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment
    • E.J. van Asselt, A.M.W.H. Thunnissen, and B.W. Dijkstra High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment J. Mol. Biol. 291 1999 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
  • 14
    • 0342901668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand
    • E.J. van Asselt, A.J. Dijkstra, K.H. Kalk, B. Takacs, W. Keck, and B.W. Dijkstra Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand Structure 7 1999 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
  • 15
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • A.M.W.H. Thunnissen, N.W. Isaacs, and B.W. Dijkstra The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes Proteins: Struct. Funct. Genet. 22 1995 245 258
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 245-258
    • Thunnissen, A.M.W.H.1    Isaacs, N.W.2    Dijkstra, B.W.3
  • 16
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • G. Davies, and B. Henrissat Structures and mechanisms of glycosyl hydrolases Structure 3 1995 853 859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 17
    • 0032512617 scopus 로고    scopus 로고
    • Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes
    • C. Evrard, J. Fastrez, and J.P. Declercq Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes J. Mol. Biol. 276 1998 151 164
    • (1998) J. Mol. Biol. , vol.276 , pp. 151-164
    • Evrard, C.1    Fastrez, J.2    Declercq, J.P.3
  • 18
    • 0035873160 scopus 로고    scopus 로고
    • Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose
    • A.K.W. Leung, H.S. Duewel, J.F. Honek, and A.M. Berghuis Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose Biochemistry 40 2001 5665 5673
    • (2001) Biochemistry , vol.40 , pp. 5665-5673
    • Leung, A.K.W.1    Duewel, H.S.2    Honek, J.F.3    Berghuis, A.M.4
  • 19
    • 0028874610 scopus 로고
    • Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism
    • A.M.W.H. Thunnissen, H.J. Rozeboom, K.H. Kalk, and B.W. Dijkstra Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism Biochemistry 34 1995 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
  • 20
    • 0034728363 scopus 로고    scopus 로고
    • Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan
    • E.J. van Asselt, K.H. Kalk, and B.W. Dijkstra Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan Biochemistry 39 2000 1924 1934
    • (2000) Biochemistry , vol.39 , pp. 1924-1934
    • Van Asselt, E.J.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 21
    • 0027979985 scopus 로고
    • Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli
    • A. Ursinus, and J.V. Höltje Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli J. Bacteriol. 176 1994 338 343
    • (1994) J. Bacteriol. , vol.176 , pp. 338-343
    • Ursinus, A.1    Höltje, J.V.2
  • 24
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • L. Holm, and C. Sander Dali: a network tool for protein structure comparison Trends Biochem. Sci. 20 1995 478 480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 25
    • 0344641932 scopus 로고    scopus 로고
    • The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition
    • M. Stoldt, J. Wohnert, O. Ohlenschlager, M. Gorlach, and L.R. Brown The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition EMBO J. 18 1999 6508 6521
    • (1999) EMBO J. , vol.18 , pp. 6508-6521
    • Stoldt, M.1    Wohnert, J.2    Ohlenschlager, O.3    Gorlach, M.4    Brown, L.R.5
  • 26
    • 14344278877 scopus 로고    scopus 로고
    • Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins
    • R. Fedorov, V. Meshcheryakov, G. Gongadze, N. Fomenkova, N. Nevskaya, and M. Selmer Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins Acta Crystallog. sect. D 57 2001 968 976
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 968-976
    • Fedorov, R.1    Meshcheryakov, V.2    Gongadze, G.3    Fomenkova, N.4    Nevskaya, N.5    Selmer, M.6
  • 28
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases
    • C. Schou, G. Rasmussen, M.B. Kaltoft, B. Henrissat, and M. Schulein Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases Eur. J. Biochem. 217 1993 947 953
    • (1993) Eur. J. Biochem. , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Kaltoft, M.B.3    Henrissat, B.4    Schulein, M.5
  • 30
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution
    • G.J. Davies, S.P. Tolley, B. Henrissat, C. Hjort, and M. Schulein Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution Biochemistry 34 1995 16210 16220
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.J.1    Tolley, S.P.2    Henrissat, B.3    Hjort, C.4    Schulein, M.5
  • 31
    • 0342335053 scopus 로고
    • The crystal structure of 1,6-anhydro-β-D-glucopyranose
    • Y.J. Park, H.S. Kim, and G.A. Jeffrey The crystal structure of 1,6-anhydro-β-D-glucopyranose Acta Crystallog. sect. B 27 1971 220 227
    • (1971) Acta Crystallog. Sect. B , vol.27 , pp. 220-227
    • Park, Y.J.1    Kim, H.S.2    Jeffrey, G.A.3
  • 32
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • D.J. Vocadlo, G.J. Davies, R. Laine, and S.G. Withers Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate Nature 412 2001 835 838
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 33
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • A.C. Terwisscha van Scheltinga, S. Armand, K.H. Kalk, A. Isogai, B. Henrissat, and B.W. Dijkstra Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis Biochemistry 34 1995 15619 15623
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 35
    • 0026666191 scopus 로고
    • Three-dimensional structure in solution of barwin, a protein from barley seed
    • S. Ludvigsen, and F.M. Poulsen Three-dimensional structure in solution of barwin, a protein from barley seed Biochemistry 31 1992 8783 8789
    • (1992) Biochemistry , vol.31 , pp. 8783-8789
    • Ludvigsen, S.1    Poulsen, F.M.2
  • 36
    • 0034699445 scopus 로고    scopus 로고
    • Loosening of plant cell walls by expansins
    • D.J. Cosgrove Loosening of plant cell walls by expansins Nature 407 2000 321 326
    • (2000) Nature , vol.407 , pp. 321-326
    • Cosgrove, D.J.1
  • 37
    • 16544394366 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli
    • K.E. van Straaten, B.W. Dijkstra, and A.M.W.H. Thunnissen Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli Acta Crystallog. sect. D 60 2004 758 760
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 758-760
    • Van Straaten, K.E.1    Dijkstra, B.W.2    Thunnissen, A.M.W.H.3
  • 38
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublié Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 39
    • 0028446542 scopus 로고
    • Expression of chicken linker histones in E. coli: Sources of problems and methods for overcoming some of the difficulties
    • S.E. Gerchman, V. Graziano, and V. Ramakrishnan Expression of chicken linker histones in E. coli: sources of problems and methods for overcoming some of the difficulties Protein Expr. Purif. 5 1994 242 251
    • (1994) Protein Expr. Purif. , vol.5 , pp. 242-251
    • Gerchman, S.E.1    Graziano, V.2    Ramakrishnan, V.3
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collection in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementations of SnB V2.0
    • C.M. Weeks, and R. Miller The design and implementations of SnB V2.0 J. Appl. Crystallog. 32 1999 120 124
    • (1999) J. Appl. Crystallog. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 42
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification and model building
    • T. Terwilliger SOLVE and RESOLVE: automated structure solution, density modification and model building J. Synchrotron Radiat. 11 2004 49 52
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 43
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 44
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
    • 0027968068 scopus 로고
    • ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson ClustalW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0018844498 scopus 로고
    • Escherichia coli murein transglycosylase. Purification by affinity chromatography and interaction with polynucleotides
    • W. Kusser, and U. Schwarz Escherichia coli murein transglycosylase. Purification by affinity chromatography and interaction with polynucleotides Eur. J. Biochem. 103 1980 277 281
    • (1980) Eur. J. Biochem. , vol.103 , pp. 277-281
    • Kusser, W.1    Schwarz, U.2
  • 49
    • 0025012287 scopus 로고
    • Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography
    • H. Harz, K. Burgdorf, and J.V. Höltje Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography Anal. Biochem. 190 1990 120 128
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Höltje, J.V.3
  • 50
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 51
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. a program for photorealistic molecular graphics
    • E.A. Merritt, and M.E. Murphy Raster3D Version 2.0. A program for photorealistic molecular graphics Acta Crystallog. sect. D 50 1994 869 873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 52
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • T.D. Fenn, D. Ringe, and G.A. Petsko POVScript+: a program for model and data visualization using persistence of vision ray-tracing J. Appl. Crystallog. 36 2003 944 947
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 53
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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