메뉴 건너뛰기




Volumn 90, Issue 2, 2013, Pages 267-277

The crystal structure of the cell division amidase amic reveals the fold of the AMIN domain, a new peptidoglycan binding domain

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL PROTEIN; PEPTIDOGLYCAN; PROTEIN AMIC; PROTEIN NLPD; UNCLASSIFIED DRUG;

EID: 84885389572     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12361     Document Type: Article
Times cited : (56)

References (40)
  • 1
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-W533.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 2
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt, T.G., and De Boer, P.A.J. (2003) The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol Microbiol 48: 1171-1182.
    • (2003) Mol Microbiol , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    De Boer, P.A.J.2
  • 3
    • 33748333182 scopus 로고    scopus 로고
    • Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli
    • Bertsche, U., Kast, T., Wolf, B., Fraipont, C., Aarsman, M.E.G., Kannenberg, K., etal. (2006) Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol Microbiol 61: 675-690.
    • (2006) Mol Microbiol , vol.61 , pp. 675-690
    • Bertsche, U.1    Kast, T.2    Wolf, B.3    Fraipont, C.4    Aarsman, M.E.G.5    Kannenberg, K.6
  • 4
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E.F., and Lutkenhaus, J. (1991) FtsZ ring structure associated with division in Escherichia coli. Nature 354: 161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 5
    • 0019511038 scopus 로고
    • Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation
    • Botta, G.A., and Park, J.T. (1981) Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation. J Bacteriol 145: 333-340.
    • (1981) J Bacteriol , vol.145 , pp. 333-340
    • Botta, G.A.1    Park, J.T.2
  • 6
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N., and Beckwith, J. (2004) A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 52: 1315-1327.
    • (2004) Mol Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 7
    • 0024335390 scopus 로고
    • Binding of d-phenylalanine and d-tyrosine to carboxypeptidase A
    • Christianson, D.W., Mangani, S., Shoham, G., and Lipscomb, W.N. (1989) Binding of d-phenylalanine and d-tyrosine to carboxypeptidase A. J Biol Chem 264: 12849-12853.
    • (1989) J Biol Chem , vol.264 , pp. 12849-12853
    • Christianson, D.W.1    Mangani, S.2    Shoham, G.3    Lipscomb, W.N.4
  • 8
    • 77953983797 scopus 로고    scopus 로고
    • A new factor stimulating peptidoglycan hydrolysis to separate daughter cells in Caulobacter crescentus
    • Collier, J. (2010) A new factor stimulating peptidoglycan hydrolysis to separate daughter cells in Caulobacter crescentus. Mol Microbiol 77: 11-14.
    • (2010) Mol Microbiol , vol.77 , pp. 11-14
    • Collier, J.1
  • 9
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin, B.D., Wang, Y., Beuria, T.K., and Margolin, W. (2007) Interaction between cell division proteins FtsE and FtsZ. J Bacteriol 189: 3026-3035.
    • (2007) J Bacteriol , vol.189 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 10
    • 54949138104 scopus 로고    scopus 로고
    • AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
    • De Souza, R.F., Anantharaman, V., De Souza, S.J., Aravind, L., and Gueiros-Filho, F.J. (2008) AMIN domains have a predicted role in localization of diverse periplasmic protein complexes. Bioinformatics 24: 2423-2426.
    • (2008) Bioinformatics , vol.24 , pp. 2423-2426
    • De Souza, R.F.1    Anantharaman, V.2    De Souza, S.J.3    Aravind, L.4    Gueiros-Filho, F.J.5
  • 12
    • 84864018985 scopus 로고    scopus 로고
    • Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli
    • Durand-Heredia, J., Rivkin, E., Fan, G., Morales, J., and Janakiraman, A. (2012) Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. J Bacteriol 194: 3189-3198.
    • (2012) J Bacteriol , vol.194 , pp. 3189-3198
    • Durand-Heredia, J.1    Rivkin, E.2    Fan, G.3    Morales, J.4    Janakiraman, A.5
  • 13
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia, J.M., Yu, H.H., De Carlo, S., Lesser, C.F., and Janakiraman, A. (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J Bacteriol 193: 1405-1413.
    • (2011) J Bacteriol , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakiraman, A.5
  • 15
    • 84855881444 scopus 로고    scopus 로고
    • FtsZ-ZapA-ZapB interactome of Escherichia coli
    • Galli, E., and Gerdes, K. (2012) FtsZ-ZapA-ZapB interactome of Escherichia coli. J Bacteriol 194: 292-302.
    • (2012) J Bacteriol , vol.194 , pp. 292-302
    • Galli, E.1    Gerdes, K.2
  • 16
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., Höltje, J.V., and Schwarz, U. (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.V.2    Schwarz, U.3
  • 17
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • Goehring, N.W., Gonzalez, M.D., and Beckwith, J. (2006) Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol Microbiol 61: 33-45.
    • (2006) Mol Microbiol , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 18
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli
    • Hale, C.A., and De Boer, P.A.J. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88: 175-185.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.J.2
  • 19
    • 0034945221 scopus 로고    scopus 로고
    • Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli
    • Heidrich, C., Templin, M.F., Ursinus, A., Merdanovic, M., Berger, J., Schwarz, H., etal. (2001) Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli. Mol Microbiol 41: 167-178.
    • (2001) Mol Microbiol , vol.41 , pp. 167-178
    • Heidrich, C.1    Templin, M.F.2    Ursinus, A.3    Merdanovic, M.4    Berger, J.5    Schwarz, H.6
  • 21
    • 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
    • Korndörfer, I.P., Danzer, J., Schmelcher, M., Zimmer, M., Skerra, A., and Loessner, M.J. (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: 678-689.
    • (2006) J Mol Biol , vol.364 , pp. 678-689
    • Korndörfer, I.P.1    Danzer, J.2    Schmelcher, M.3    Zimmer, M.4    Skerra, A.5    Loessner, M.J.6
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 71649092785 scopus 로고    scopus 로고
    • Processing diffraction data with mosflm
    • Read, R.J., and Sussman, J.L. (eds). Dordrecht: Springer Netherlands
    • Leslie, A.G.W., and Powell, H.R. (2007) Processing diffraction data with mosflm. In Evolving Methods for Macromolecular Crystallography. Read, R.J., and Sussman, J.L. (eds). Dordrecht: Springer Netherlands, pp. 41-51.
    • (2007) Evolving Methods for Macromolecular Crystallography , pp. 41-51
    • Leslie, A.G.W.1    Powell, H.R.2
  • 24
    • 80053609598 scopus 로고    scopus 로고
    • Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range
    • Mayer, M.J., Garefalaki, V., Spoerl, R., Narbad, A., and Meijers, R. (2011) Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range. J Bacteriol 193: 5477-5486.
    • (2011) J Bacteriol , vol.193 , pp. 5477-5486
    • Mayer, M.J.1    Garefalaki, V.2    Spoerl, R.3    Narbad, A.4    Meijers, R.5
  • 25
    • 77953996215 scopus 로고    scopus 로고
    • DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus
    • Möll, A., Schlimpert, S., Briegel, A., Jensen, G.J., and Thanbichler, M. (2010) DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus. Mol Microbiol 77: 90-107.
    • (2010) Mol Microbiol , vol.77 , pp. 90-107
    • Möll, A.1    Schlimpert, S.2    Briegel, A.3    Jensen, G.J.4    Thanbichler, M.5
  • 26
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R.J., Perrakis, A., and Lamzin, V.S. (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374: 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 27
    • 37548998632 scopus 로고    scopus 로고
    • The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli
    • Müller, P., Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E., etal. (2007) The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli. J Biol Chem 282: 36394-36402.
    • (2007) J Biol Chem , vol.282 , pp. 36394-36402
    • Müller, P.1    Ewers, C.2    Bertsche, U.3    Anstett, M.4    Kallis, T.5    Breukink, E.6
  • 28
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau, C., Markovski, M., Uehara, T., Lupoli, T.J., Walker, S., Kahne, D.E., and Bernhardt, T.G. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5    Kahne, D.E.6    Bernhardt, T.G.7
  • 29
    • 80052525834 scopus 로고    scopus 로고
    • A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators
    • Peters, N.T., Dinh, T., and Bernhardt, T.G. (2011) A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators. J Bacteriol 193: 4973-4983.
    • (2011) J Bacteriol , vol.193 , pp. 4973-4983
    • Peters, N.T.1    Dinh, T.2    Bernhardt, T.G.3
  • 30
    • 84881550004 scopus 로고    scopus 로고
    • Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site
    • Peters, N.T., Morlot, C., Yang, D.C., Uehara, T., Vernet, T., and Bernhardt, T.G. (2013) Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site. Mol Microbiol 89: 690-701.
    • (2013) Mol Microbiol , vol.89 , pp. 690-701
    • Peters, N.T.1    Morlot, C.2    Yang, D.C.3    Uehara, T.4    Vernet, T.5    Bernhardt, T.G.6
  • 32
    • 77953977302 scopus 로고    scopus 로고
    • A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains
    • Poggio, S., Takacs, C.N., Vollmer, W., and Jacobs-Wagner, C. (2010) A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains. Mol Microbiol 77: 74-89.
    • (2010) Mol Microbiol , vol.77 , pp. 74-89
    • Poggio, S.1    Takacs, C.N.2    Vollmer, W.3    Jacobs-Wagner, C.4
  • 33
    • 0013096299 scopus 로고
    • Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12
    • Spratt, B.G. (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci USA 72: 2999-3003.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 34
    • 77953265009 scopus 로고    scopus 로고
    • Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization
    • Sycuro, L.K., Pincus, Z., Gutierrez, K.D., Biboy, J., Stern, C.A., Vollmer, W., and Salama, N.R. (2010) Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. Cell 141: 822-833.
    • (2010) Cell , vol.141 , pp. 822-833
    • Sycuro, L.K.1    Pincus, Z.2    Gutierrez, K.D.3    Biboy, J.4    Stern, C.A.5    Vollmer, W.6    Salama, N.R.7
  • 36
    • 67749117916 scopus 로고    scopus 로고
    • LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli
    • Uehara, T., Dinh, T., and Bernhardt, T.G. (2009) LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J Bacteriol 191: 5094-5107.
    • (2009) J Bacteriol , vol.191 , pp. 5094-5107
    • Uehara, T.1    Dinh, T.2    Bernhardt, T.G.3
  • 37
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara, T., Parzych, K.R., Dinh, T., and Bernhardt, T.G. (2010) Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29: 1412-1422.
    • (2010) EMBO J , vol.29 , pp. 1412-1422
    • Uehara, T.1    Parzych, K.R.2    Dinh, T.3    Bernhardt, T.G.4
  • 38
    • 0000330205 scopus 로고    scopus 로고
    • On the use of the merging R factor as a quality indicator for X-ray data
    • Weiss, M.S., and Hilgenfeld, R. (1997) On the use of the merging R factor as a quality indicator for X-ray data. J Appl Crystallogr 30: 203-205.
    • (1997) J Appl Crystallogr , vol.30 , pp. 203-205
    • Weiss, M.S.1    Hilgenfeld, R.2
  • 39
    • 81055145336 scopus 로고    scopus 로고
    • An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
    • Yang, D.C., Peters, N.T., Parzych, K.R., Uehara, T., Markovski, M., and Bernhardt, T.G. (2011) An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring. Proc Natl Acad Sci USA 108: 18209-18210.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18209-18210
    • Yang, D.C.1    Peters, N.T.2    Parzych, K.R.3    Uehara, T.4    Markovski, M.5    Bernhardt, T.G.6
  • 40
    • 84864816426 scopus 로고    scopus 로고
    • A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division
    • Yang, D.C., Tan, K., Joachimiak, A., and Bernhardt, T.G. (2012) A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division. Mol Microbiol 85: 768-781.
    • (2012) Mol Microbiol , vol.85 , pp. 768-781
    • Yang, D.C.1    Tan, K.2    Joachimiak, A.3    Bernhardt, T.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.