메뉴 건너뛰기




Volumn 5, Issue 1, 2014, Pages

Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; DIMER; PEPTIDOGLYCAN; PROTEIN LYTA; UNCLASSIFIED DRUG;

EID: 84903370963     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01120-13     Document Type: Article
Times cited : (50)

References (36)
  • 1
    • 0005413121 scopus 로고
    • Mechanism of action of penicillin: Triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis
    • Tomasz A, Waks S. 1975. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc. Natl. Acad. Sci. U. S. A. 72:4162-4166. http://dx.doi.org/10.1073/ pnas.72.10.4162.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 4162-4166
    • Tomasz, A.1    Waks, S.2
  • 2
    • 40549088892 scopus 로고    scopus 로고
    • Streptococcus pneumoniae deficient in pneumolysin or autolysin has reduced virulence in meningitis
    • Hirst RA, Gosai B, Rutman A, Guerin CJ, Nicotera P, Andrew PW, O'Callaghan C. 2008. Streptococcus pneumoniae deficient in pneumolysin or autolysin has reduced virulence in meningitis. J. Infect. Dis. 197: 744-751. http://dx.doi.org/10.1086/527322.
    • (2008) J. Infect. Dis. , vol.197 , pp. 744-751
    • Hirst, R.A.1    Gosai, B.2    Rutman, A.3    Guerin, C.J.4    Nicotera, P.5    Andrew, P.W.6    O'Callaghan, C.7
  • 3
    • 0022425319 scopus 로고
    • Interaction of the pneumococcal amidase with lipoteichoic acid and choline
    • Briese T, Hakenbeck R. 1985. Interaction of the pneumococcal amidase with lipoteichoic acid and choline. Eur. J. Biochem. 146:417-427. http:// dx.doi.org/10.1111/j.1432-1033.1985.tb08668.x.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 417-427
    • Briese, T.1    Hakenbeck, R.2
  • 4
    • 69049097139 scopus 로고    scopus 로고
    • Streptococcus pneumoniae autolysis prevents phagocytosis and production of phagocyte-activating cytokines
    • Martner A, Skovbjerg S, Paton JC, Wold AE. 2009. Streptococcus pneumoniae autolysis prevents phagocytosis and production of phagocyte-activating cytokines. Infect. Immun. 77:3826-3837. http:// dx.doi.org/10.1128/IAI.00290-09.
    • (2009) Infect. Immun. , vol.77 , pp. 3826-3837
    • Martner, A.1    Skovbjerg, S.2    Paton, J.C.3    Wold, A.E.4
  • 5
    • 0024205130 scopus 로고
    • Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae
    • Tomasz A, Moreillon P, Pozzi G. 1988. Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae. J. Bacteriol. 170: 5931-5934.
    • (1988) J. Bacteriol. , vol.170 , pp. 5931-5934
    • Tomasz, A.1    Moreillon, P.2    Pozzi, G.3
  • 7
    • 0028223308 scopus 로고
    • The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase
    • Cheng X, Zhang X, Pflugrath JW, Studier FW. 1994. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 91:4034-4038. http:// dx.doi.org/10.1073/pnas.91.9.4034.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4034-4038
    • Cheng, X.1    Zhang, X.2    Pflugrath, J.W.3    Studier, F.W.4
  • 8
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding MM. 2001. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D Biol. Crystallogr. 57:401-411. http://dx.doi.org/ 10.1107/S0907444900019168.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 9
    • 77950423334 scopus 로고    scopus 로고
    • Structural basis of cell wall cleavage by a staphylococcal autolysin
    • Zoll S, Pätzold B, Schlag M, Götz F, Kalbacher H, Stehle T. 2010. Structural basis of cell wall cleavage by a staphylococcal autolysin. PLoS Pathog. 6:e1000807. http://dx.doi.org/10.1371/journal.ppat.1000807.
    • (2010) PLoS Pathog. , vol.6
    • Zoll, S.1    Pätzold, B.2    Schlag, M.3    Götz, F.4    Kalbacher, H.5    Stehle, T.6
  • 11
    • 34547118354 scopus 로고    scopus 로고
    • Key role of amino acid residues in the dimerization and catalytic activation of the autolysin LytA, an important virulence factor in Streptococcus pneumoniae
    • Romero P, López R, García E. 2007. Key role of amino acid residues in the dimerization and catalytic activation of the autolysin LytA, an important virulence factor in Streptococcus pneumoniae. J. Biol. Chem. 282: 17729-17737. http://dx.doi.org/10.1074/jbc.M611795200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17729-17737
    • Romero, P.1    López, R.2    García, E.3
  • 13
    • 0036349994 scopus 로고    scopus 로고
    • Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: Insights into the dynamics of the active homodimer
    • Fernández-Tornero C, García E, López R, Giménez-Gallego G, Romero A. 2002. Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer. J. Mol. Biol. 321:163-173. http://dx.doi.org/10.1016/S0022-2836(02)00596-X.
    • (2002) J. Mol. Biol. , vol.321 , pp. 163-173
    • Fernández-Tornero, C.1    García, E.2    López, R.3    Giménez-Gallego, G.4    Romero, A.5
  • 14
    • 0035186065 scopus 로고    scopus 로고
    • A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA
    • Fernández-Tornero C, López R, García E, Giménez-Gallego G, Romero A. 2001. A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA. Nat. Struct. Biol. 8:1020-1024. http://dx.doi.org/10.1038/nsb724.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1020-1024
    • Fernández-Tornero, C.1    López, R.2    García, E.3    Giménez-Gallego, G.4    Romero, A.5
  • 17
    • 0036724742 scopus 로고    scopus 로고
    • Purification and polar localization of pneumococcal LytB, a putative endo-beta-Nacetylglucosaminidase: The chain-dispersing murein hydrolase
    • De Las Rivas B, García JL, López R, García P. 2002. Purification and polar localization of pneumococcal LytB, a putative endo-beta-Nacetylglucosaminidase: the chain-dispersing murein hydrolase. J. Bacteriol. 184:4988-5000. http://dx.doi.org/10.1128/JB.184.18.4988-5000.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 4988-5000
    • De Las Rivas, B.1    García, J.L.2    López, R.3    García, P.4
  • 18
    • 0024575183 scopus 로고
    • Subcellular localization of the major pneumococcal autolysin: A peculiar mechanism of secretion in Escherichia coli
    • Díaz E, García E, Ascaso C, Méndez E, López R, García JL. 1989. Subcellular localization of the major pneumococcal autolysin: a peculiar mechanism of secretion in Escherichia coli. J. Biol. Chem. 264:1238-1244.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1238-1244
    • Díaz, E.1    García, E.2    Ascaso, C.3    Méndez, E.4    López, R.5    García, J.L.6
  • 20
    • 84866338446 scopus 로고    scopus 로고
    • Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition
    • Zoll S, Schlag M, Shkumatov AV, Rautenberg M, Svergun DI, Götz F, Stehle T. 2012. Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition. J. Bacteriol. 194:3789-3802. http://dx.doi.org/10.1128/JB.00331-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 3789-3802
    • Zoll, S.1    Schlag, M.2    Shkumatov, A.V.3    Rautenberg, M.4    Svergun, D.I.5    Götz, F.6    Stehle, T.7
  • 21
    • 0027181992 scopus 로고
    • Teichoic acid and lipoteichoic acid of Streptococcus pneumoniae possess identical chain structures. A reinvestigation of teichoid acid (C polysaccharide)
    • Fischer W, Behr T, Hartmann R, Peter-Katalinić J, Egge H. 1993. Teichoic acid and lipoteichoic acid of Streptococcus pneumoniae possess identical chain structures. A reinvestigation of teichoid acid (C polysaccharide). Eur. J. Biochem. 215:851-857. http://dx.doi.org/10.1111/ j.1432-1033.1993.tb18102.x.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 851-857
    • Fischer, W.1    Behr, T.2    Hartmann, R.3    Peter-Katalinić, J.4    Egge, H.5
  • 22
    • 84884580019 scopus 로고    scopus 로고
    • Effects of low PBP2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6
    • Berg KH, Stamsås GA, Straume D, Håvarstein LS. 2013. Effects of low PBP2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6. J. Bacteriol. 195:4342-4354. http:// dx.doi.org/10.1128/JB.00184-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 4342-4354
    • Berg, K.H.1    Stamsås, G.A.2    Straume, D.3    Håvarstein, L.S.4
  • 23
    • 1642355320 scopus 로고    scopus 로고
    • Synthesis of a fragment of bacterial cell wall
    • Hesek D, Lee M, Morio K, Mobashery S. 2004. Synthesis of a fragment of bacterial cell wall. J. Org. Chem. 69:2137-2146. http://dx.doi.org/ 10.1021/jo035583k.
    • (2004) J. Org. Chem. , vol.69 , pp. 2137-2146
    • Hesek, D.1    Lee, M.2    Morio, K.3    Mobashery, S.4
  • 24
    • 0842328947 scopus 로고    scopus 로고
    • Synthetic peptidoglycan substrates for penicillinbinding protein 5 of gram-negative bacteria
    • Hesek D, Suvorov M, Morio K, Lee M, Brown S, Vakulenko SB, Mobashery S. 2004. Synthetic peptidoglycan substrates for penicillinbinding protein 5 of gram-negative bacteria. J. Org. Chem. 69:778-784. http://dx.doi.org/10.1021/jo035397e.
    • (2004) J. Org. Chem. , vol.69 , pp. 778-784
    • Hesek, D.1    Suvorov, M.2    Morio, K.3    Lee, M.4    Brown, S.5    Vakulenko, S.B.6    Mobashery, S.7
  • 26
    • 84863643938 scopus 로고    scopus 로고
    • Automated acquisition and analysis of small angle X-ray scattering data
    • Franke D, Kikhney AG, Svergun DI. 2012. Automated acquisition and analysis of small angle X-ray scattering data. Nucl. Instrum. Methods Phys. Res. A 689:52-59. http://dx.doi.org/10.1016/j.nima.2012.06.008.
    • (2012) Nucl. Instrum. Methods Phys. Res. A , vol.689 , pp. 52-59
    • Franke, D.1    Kikhney, A.G.2    Svergun, D.I.3
  • 27
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux très pétits angles: Application à l'etude de phénomènes ultramicroscopiques
    • Guinier A. 1939. La diffraction des rayons X aux très pétits angles: application à l'etude de phénomènes ultramicroscopiques. Ann. Phys. 12:67.
    • (1939) Ann. Phys. , vol.12 , pp. 67
    • Guinier, A.1
  • 28
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25:495-503. http://dx.doi.org/10.1107/S0021889892001663.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 29
    • 80052446729 scopus 로고    scopus 로고
    • Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism
    • Carrasco-Lopez C, Rojas-Altuve A, et al. 2011. Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism. J. Biol. Chem. 286(36):31714-31722.
    • (2011) J. Biol. Chem. , vol.286 , Issue.36 , pp. 31714-31722
    • Carrasco-Lopez, C.1    Rojas-Altuve, A.2
  • 30
    • 33646140122 scopus 로고    scopus 로고
    • Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria
    • Guan R, Brown PH, et al. 2006. Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria. Protein Sci. 15(5):1199-1206.
    • (2006) Protein Sci. , vol.15 , Issue.5 , pp. 1199-1206
    • Guan, R.1    Brown, P.H.2
  • 31
    • 10344259137 scopus 로고    scopus 로고
    • Structural basis for peptidoglycan binding by peptidoglycan recognition proteins
    • Guan R, Roychowdhury A, et al. 2004. Structural basis for peptidoglycan binding by peptidoglycan recognition proteins. Proc. Natl. Acad. Sci. U. S. A. 101(49):17168-17173.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.49 , pp. 17168-17173
    • Guan, R.1    Roychowdhury, A.2
  • 32
    • 77249102992 scopus 로고    scopus 로고
    • Specific structural features of the N-acetylmuramoyl-L-alanine amidase AmiD from Escherichia coli and mechanistic implications for enzymes of this family
    • Kerff F, Petrella S, et al. 2010. Specific structural features of the N-acetylmuramoyl-L-alanine amidase AmiD from Escherichia coli and mechanistic implications for enzymes of this family. J. Mol. Biol. 397(1): 249-259.
    • (2010) J. Mol. Biol. , vol.397 , Issue.1 , pp. 249-259
    • Kerff, F.1    Petrella, S.2
  • 33
    • 33751066117 scopus 로고    scopus 로고
    • The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls
    • Korndorfer IP, Danzer J, et al. 2006. The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls. J. Mol. Biol. 364(4):678-689.
    • (2006) J. Mol. Biol. , vol.364 , Issue.4 , pp. 678-689
    • Korndorfer, I.P.1    Danzer, J.2
  • 34
    • 80053201228 scopus 로고    scopus 로고
    • Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins
    • Low LY, Yang C, et al. 2011. Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins. J. Biol. Chem. 286(39):34391-34403.
    • (2011) J. Biol. Chem. , vol.286 , Issue.39 , pp. 34391-34403
    • Low, L.Y.1    Yang, C.2
  • 35
    • 27444432629 scopus 로고    scopus 로고
    • Structure and lytic activity of a Bacillus anthracis prophage endolysin
    • Low LY, Yang C, et al. 2005. Structure and lytic activity of a Bacillus anthracis prophage endolysin. J. Biol. Chem. 280(42):35433-35439.
    • (2005) J. Biol. Chem. , vol.280 , Issue.42 , pp. 35433-35439
    • Low, L.Y.1    Yang, C.2
  • 36
    • 0000331730 scopus 로고
    • A study of the genetic material determining an enzyme in Pneumococcus
    • Lacks S, Hotchkiss RD. 1960. A study of the genetic material determining an enzyme in Pneumococcus. Biochim. Biophys. Acta 39:508-518.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 508-518
    • Lacks, S.1    Hotchkiss, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.