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Volumn 194, Issue 17, 2012, Pages 4537-4545

Crystal structure of the catalytic domain of the Bacillus cereus SleB protein, important in cortex peptidoglycan degradation during spore germination

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLUTAMIC ACID; GLUTAMINE; GLYCOSYLTRANSFERASE; PEPTIDOGLYCAN; SLEB PROTEIN; UNCLASSIFIED DRUG;

EID: 84866315691     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00877-12     Document Type: Article
Times cited : (37)

References (57)
  • 1
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: building new software for automated crystallographic structure determination
    • Adams PD, et al.PNIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58:1948-1954.
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 2
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn NT, Clarke AJ. 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
  • 3
    • 0033979067 scopus 로고    scopus 로고
    • Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB
    • Boland FM, Atrih A, Chirakkal H, Foster SJ, Moir A. 2000. Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB. Microbiology 146:57-64.
    • (2000) Microbiology , vol.146 , pp. 57-64
    • Boland, F.M.1    Atrih, A.2    Chirakkal, H.3    Foster, S.J.4    Moir, A.5
  • 4
    • 0028975575 scopus 로고
    • Revival and identification of bacterial spores in 25-to 40-million-year-old Dominican amber
    • Cano RJ, Borucki MK. 1995. Revival and identification of bacterial spores in 25-to 40-million-year-old Dominican amber. Science 268:1060-1064.
    • (1995) Science , vol.268 , pp. 1060-1064
    • Cano, R.J.1    Borucki, M.K.2
  • 5
    • 0036667425 scopus 로고    scopus 로고
    • Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination
    • Chirakkal H, O'Rourke M, Atrih A, Foster SJ, Moir A. 2002. Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination. Microbiology 148:2383-2392.
    • (2002) Microbiology , vol.148 , pp. 2383-2392
    • Chirakkal, H.1    O'rourke, M.2    Atrih, A.3    Foster, S.J.4    Moir, A.5
  • 6
    • 77957853839 scopus 로고    scopus 로고
    • Mutational analysis of Bacillus megaterium QM B1551 cortex-lytic enzymes
    • Christie G, Ustok FI, Lu Q, Packman LC, Lowe CR. 2010. Mutational analysis of Bacillus megaterium QM B1551 cortex-lytic enzymes. J. Bacteriol.192:5378-5389.
    • (2010) J. Bacteriol. , vol.192 , pp. 5378-5389
    • Christie, G.1    Ustok, F.I.2    Lu, Q.3    Packman, L.C.4    Lowe, C.R.5
  • 8
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. 2007. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35:W375-W383.
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 9
    • 46049095480 scopus 로고    scopus 로고
    • Cortex peptidoglycan lytic activity in germinating Bacillus anthracis spores
    • Dowd MM, Orsburn B, Popham DL. 2008. Cortex peptidoglycan lytic activity in germinating Bacillus anthracis spores. J. Bacteriol. 190:4541-4548.
    • (2008) J. Bacteriol. , vol.190 , pp. 4541-4548
    • Dowd, M.M.1    Orsburn, B.2    Popham, D.L.3
  • 12
    • 69949106986 scopus 로고    scopus 로고
    • The germinationspecific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence
    • Giebel JD, Carr KA, Anderson EC, Hanna PC. 2009. The germinationspecific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence. J. Bacteriol. 191:5569-5576.
    • (2009) J. Bacteriol. , vol.191 , pp. 5569-5576
    • Giebel, J.D.1    Carr, K.A.2    Anderson, E.C.3    Hanna, P.C.4
  • 13
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCRdriven overlap extension
    • Heckman KL, Pease LR. 2007. Gene splicing and mutagenesis by PCRdriven overlap extension. Nat. Protoc. 2:924-932.
    • (2007) Nat. Protoc. , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 14
    • 75149124883 scopus 로고    scopus 로고
    • Contributions of four cortex lytic enzymes to germination of Bacillus anthracis spores
    • Heffron JD, Lambert EA, Sherry N, Popham DL. 2010. Contributions of four cortex lytic enzymes to germination of Bacillus anthracis spores. J. Bacteriol. 192:763-770.
    • (2010) J. Bacteriol. , vol.192 , pp. 763-770
    • Heffron, J.D.1    Lambert, E.A.2    Sherry, N.3    Popham, D.L.4
  • 15
    • 64049117377 scopus 로고    scopus 로고
    • Roles of germinationspecific lytic enzymes CwlJ and SleB in Bacillus anthracis
    • Heffron JD, Orsburn B, Popham DL. 2009. Roles of germinationspecific lytic enzymes CwlJ and SleB in Bacillus anthracis. J. Bacteriol. 191:2237-2247.
    • (2009) J. Bacteriol. , vol.191 , pp. 2237-2247
    • Heffron, J.D.1    Orsburn, B.2    Popham, D.L.3
  • 16
    • 78650122220 scopus 로고    scopus 로고
    • In vitro studies of peptidoglycan binding and hydrolysis by the Bacillus anthracis germination-specific lytic enzyme SleB
    • Heffron JD, Sherry N, Popham DL. 2011. In vitro studies of peptidoglycan binding and hydrolysis by the Bacillus anthracis germination-specific lytic enzyme SleB. J. Bacteriol. 193:125-131.
    • (2011) J. Bacteriol. , vol.193 , pp. 125-131
    • Heffron, J.D.1    Sherry, N.2    Popham, D.L.3
  • 18
    • 33947408762 scopus 로고    scopus 로고
    • Cloning and identification of a gene encoding spore cortex-lytic enzyme in Bacillus thuringiensis
    • Hu K, Yang H, Liu G, Tan H. 2007. Cloning and identification of a gene encoding spore cortex-lytic enzyme in Bacillus thuringiensis. Curr. Microbiol. 54:292-295.
    • (2007) Curr. Microbiol. , vol.54 , pp. 292-295
    • Hu, K.1    Yang, H.2    Liu, G.3    Tan, H.4
  • 19
    • 0031941630 scopus 로고    scopus 로고
    • Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores
    • Ishikawa S, Yamane K, Sekiguchi J. 1998. Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores. J. Bacteriol. 180:1375-1380.
    • (1998) J. Bacteriol. , vol.180 , pp. 1375-1380
    • Ishikawa, S.1    Yamane, K.2    Sekiguchi, J.3
  • 20
    • 0018570657 scopus 로고
    • X-ray crystallography of the binding of the bacterial cell wall trisaccharideNAMNAG-NAM to lysozyme
    • Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC. 1979. X-ray crystallography of the binding of the bacterial cell wall trisaccharideNAMNAG-NAM to lysozyme. Nature 282:875-878.
    • (1979) Nature , vol.282 , pp. 875-878
    • Kelly, J.A.1    Sielecki, A.R.2    Sykes, B.D.3    James, M.N.4    Phillips, D.C.5
  • 21
    • 0028152536 scopus 로고
    • Preservation records of micro-organisms: evidence of the tenacity of life
    • Kennedy MJ, Reader SL, Swierczynski LM. 1994. Preservation records of micro-organisms: evidence of the tenacity of life. Microbiology 140:2513-2529.
    • (1994) Microbiology , vol.140 , pp. 2513-2529
    • Kennedy, M.J.1    Reader, S.L.2    Swierczynski, L.M.3
  • 22
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: a server for predicting protein function from 3D structure
    • Laskowski RA, Watson JD, Thornton JM. 2005. ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res. 33:W89-W93.
    • (2005) Nucleic Acids Res. , vol.33
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 24
    • 33747187232 scopus 로고    scopus 로고
    • Subcellular localization of a germinationspecific cortex-lytic enzyme, SleB, of Bacilli during sporulation
    • Masayama A, et al. 2006. Subcellular localization of a germinationspecific cortex-lytic enzyme, SleB, of Bacilli during sporulation. Genes Genet. Syst. 81:163-169.
    • (2006) Genes Genet. Syst. , vol.81 , pp. 163-169
    • Msayama, A.1
  • 25
    • 33747106140 scopus 로고    scopus 로고
    • How do spores germinate?
    • Moir A. 2006. How do spores germinate? J. Appl. Microbiol. 101:526-530.
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 526-530
    • Moir, A.1
  • 26
    • 0032931055 scopus 로고    scopus 로고
    • Expression of a germination-specific amidase, SleB, of Bacilli in the forespore compartment of sporulating cells and its localization on the exterior side of the cortex in dormant spores
    • Moriyama R, et al. 1999. Expression of a germination-specific amidase, SleB, of Bacilli in the forespore compartment of sporulating cells and its localization on the exterior side of the cortex in dormant spores. J. Bacteriol.181:2373-2378.
    • (1999) J. Bacteriol. , vol.181 , pp. 2373-2378
    • Moriyama, R.1
  • 27
    • 0029832937 scopus 로고    scopus 로고
    • A germination-specific spore cortex-lytic enzyme from Bacillus cereus spores: cloning and sequencing of the gene and molecular characterization of the enzyme
    • Moriyama R, et al. 1996. A germination-specific spore cortex-lytic enzyme from Bacillus cereus spores: cloning and sequencing of the gene and molecular characterization of the enzyme. J. Bacteriol. 178:5330-5332.
    • (1996) J. Bacteriol. , vol.178 , pp. 5330-5332
    • Moriyama, R.1
  • 30
    • 0030777303 scopus 로고    scopus 로고
    • CATH-a hierarchic classification of protein domain structures
    • Orengo CA, et al. 1997. CATH-a hierarchic classification of protein domain structures. Structure 5:1093-1108.
    • (1997) Structure , vol.5 , pp. 1093-1108
    • Orengo, C.A.1
  • 31
    • 0036839162 scopus 로고    scopus 로고
    • MAMMOTH (matching molecular models obtained from theory): an automated method for model comparison
    • Ortiz AR, Strauss CE, Olmea O. 2002. MAMMOTH (matching molecular models obtained from theory): an automated method for model comparison.Protein Sci. 11:2606-2621.
    • (2002) Protein Sci. , vol.11 , pp. 2606-2621
    • Ortiz, A.R.1    Strauss, C.E.2    Olmea, O.3
  • 32
    • 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
  • 34
    • 0033797695 scopus 로고    scopus 로고
    • Characterization of spores of Bacillus subtilis which lack dipicolinic acid
    • Paidhungat M, Setlow B, Driks A, Setlow P. 2000. Characterization of spores of Bacillus subtilis which lack dipicolinic acid. J. Bacteriol. 182: 5505-5512.
    • (2000) J. Bacteriol. , vol.182 , pp. 5505-5512
    • Paidhungat, M.1    Setlow, B.2    Driks, A.3    Setlow, P.4
  • 35
    • 0034972414 scopus 로고    scopus 로고
    • Localization of a germinant receptor protein (GerBA) to the inner membrane of Bacillus subtilis spores
    • Paidhungat M, Setlow P. 2001. Localization of a germinant receptor protein (GerBA) to the inner membrane of Bacillus subtilis spores. J. Bacteriol. 183:3982-3990.
    • (2001) J. Bacteriol. , vol.183 , pp. 3982-3990
    • Paidhungat, M.1    Setlow, P.2
  • 36
    • 79952465087 scopus 로고    scopus 로고
    • Germination of spores of Bacillales and Clostridiales species: mechanisms and proteins involved
    • Paredes-Sabja D, Setlow P, Sarker MR. 2011. Germination of spores of Bacillales and Clostridiales species: mechanisms and proteins involved.Trends Microbiol. 19:85-94.
    • (2011) Trends Microbiol. , vol.19 , pp. 85-94
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 37
    • 0036203186 scopus 로고    scopus 로고
    • Specialized peptidoglycan of the bacterial endospore: the inner wall of the lockbox
    • Popham DL. 2002. Specialized peptidoglycan of the bacterial endospore: the inner wall of the lockbox. Cell. Mol. Life Sci. 59:426-433.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 426-433
    • Popham, D.L.1
  • 40
    • 66849118916 scopus 로고    scopus 로고
    • Characterization of the germination of Bacillus megaterium spores lacking enzymes that degrade the spore cortex
    • Setlow B, et al. 2009. Characterization of the germination of Bacillus megaterium spores lacking enzymes that degrade the spore cortex. J. Appl. Microbiol. 107:318-328.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 318-328
    • Setlow, B.1
  • 42
    • 33744733251 scopus 로고    scopus 로고
    • Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals
    • Setlow P. 2006. Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals. J. Appl. Microbiol. 101:514-525.
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 514-525
    • Setlow, P.1
  • 43
    • 0002664570 scopus 로고    scopus 로고
    • Spores and their significance
    • In Doyle MP, Buchanan R (ed), Food microbiology: fundamentals and frontiers. ASM Press, Washington, DC
    • Setlow P, Johnson EA. 2007. Spores and their significance, p 35-67. In Doyle MP, Buchanan R (ed), Food microbiology: fundamentals and frontiers.ASM Press, Washington, DC.
    • (2007) , pp. 35-67
    • Setlow, P.1    Johnson, E.A.2
  • 44
    • 0029931070 scopus 로고    scopus 로고
    • Structure of cyclodextrin glycosyltransferas complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity
    • Strokopytov B, et al. 1996. Structure of cyclodextrin glycosyltransferasecomplexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity. Biochemistry 35:4241-4249.
    • (1996) Biochemistry , vol.35 , pp. 4241-4249
    • Strokopytov, B.1
  • 46
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW.1994. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2:1181-1189.
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Scheltinga, A.C.T.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 47
    • 0028091202 scopus 로고
    • Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography
    • Thunnissen AM, et al. 1994. Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography. Nature 367:750-753.
    • (1994) Nature , vol.367 , pp. 750-753
    • Thunnissen, A.M.1
  • 48
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • Thunnissen AM, Isaacs NW, Dijkstra BW. 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.1    Isaacs, N.W.2    Dijkstra, B.W.3
  • 49
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31:455-461.
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 50
    • 0342901668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EFhand
    • van Asselt EJ, et al. 1999. Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EFhand. Structure 7:1167-1180.
    • (1999) Structure , vol.7 , pp. 1167-1180
    • Asselt, E.J.V.1
  • 51
    • 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 EJ, Thunnissen AM, Dijkstra BW. 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
    • Asselt, E.J.V.1    Thunnissen, A.M.2    Dijkstra, B.W.3
  • 52
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J. 1993. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229:105-124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Duyne, G.D.V.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 53
    • 0034687374 scopus 로고    scopus 로고
    • Isolation of a 250 million-year-old halotolerant bacterium from a primary salt crystal
    • Vreeland RH, Rosenzweig WD, Powers DW. 2000. Isolation of a 250 million-year-old halotolerant bacterium from a primary salt crystal. Nature 407:897-900.
    • (2000) Nature , vol.407 , pp. 897-900
    • Vreeland, R.H.1    Rosenzweig, W.D.2    Powers, D.W.3
  • 54
    • 0028794520 scopus 로고
    • The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue
    • Weaver LH, Grutter MG, Matthews BW. 1995. The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J. Mol. Biol. 245:54-68.
    • (1995) J. Mol. Biol. , vol.245 , pp. 54-68
    • Weaver, L.H.1    Grutter, M.G.2    Matthews, B.W.3
  • 55
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ. 2003. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374: 300-321.
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 56
    • 84871967847 scopus 로고    scopus 로고
    • Preferential binding of allosteric modulators to active and inactive conformational states of metabotropic glutamate receptors
    • doi:10.1186/1471-2105-9-S1-S16
    • Yanamala N, Tirupula KC, Klein-Seetharaman J. 2008. Preferential binding of allosteric modulators to active and inactive conformational states of metabotropic glutamate receptors.BMCBioinformatics 9(Suppl.1):S16. doi:10.1186/1471-2105-9-S1-S16.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPP.1
    • Yanamala, N.1    Tirupula, K.C.2    Klein-Seetharaman, J.3
  • 57
    • 77954351126 scopus 로고    scopus 로고
    • Studies of the commitment step in the germination of spores of Bacillus species
    • Yi X, Setlow P. 2010. Studies of the commitment step in the germination of spores of Bacillus species. J. Bacteriol. 192:3424-3433.
    • (2010) J. Bacteriol. , vol.192 , pp. 3424-3433
    • Yi, X.1    Setlow, P.2


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