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Volumn 289, Issue 27, 2014, Pages 19245-19253

Structural insights into the lipoprotein outer membrane regulator of penicillin-binding protein 1B

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

EID: 84903848142     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.565879     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas, A., Banzhaf, M., Gross, C. A., and Vollmer, W. (2012) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol. 10, 123-136
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 2
    • 84867040298 scopus 로고    scopus 로고
    • (Dougherty, T. J., and Pucci, M. J., eds), Springer Science-Business Media, Basel
    • Page, M. P. (2012) in Antibiotic Discovery and Development (Dougherty, T. J., and Pucci, M. J., eds) pp. 79-117, Springer Science-Business Media, Basel
    • (2012) Antibiotic Discovery and Development , pp. 79-117
    • Page, M.P.1
  • 3
    • 84885848816 scopus 로고    scopus 로고
    • Fortifying the wall: Synthesis, regulation and degradation of bacterial peptidoglycan
    • Sobhanifar, S., King, D. T., and Strynadka, N. C. (2013) Fortifying the wall: synthesis, regulation and degradation of bacterial peptidoglycan. Curr. Opin. Struct. Biol. 23, 695-703
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 695-703
    • Sobhanifar, S.1    King, D.T.2    Strynadka, N.C.3
  • 6
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell Wall synthesis machinery and mreb filaments in B. Subtilis
    • Garner, E. C., Bernard, R., Wang, W., Zhuang, X., Rudner, D. Z., and Mitchison, T. (2011) Coupled, circumferential motions of the cell Wall synthesis machinery and MreB filaments in B. subtilis. Science 333, 222-225
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 7
    • 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
  • 9
    • 84892141401 scopus 로고    scopus 로고
    • Lipoprotein activators stimulate Escherichia coli penicillinbinding proteins by different mechanisms
    • Lupoli, T. J., Lebar, M. D., Markovski, M., Bernhardt, T., Kahne, D., and Walker, S. (2014) Lipoprotein activators stimulate Escherichia coli penicillinbinding proteins by different mechanisms. J. Am. Chem. Soc. 136, 52-55
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 52-55
    • Lupoli, T.J.1    Lebar, M.D.2    Markovski, M.3    Bernhardt, T.4    Kahne, D.5    Walker, S.6
  • 10
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. Coli
    • Gerding, M. A., Ogata, Y., Pecora, N. D., Niki, H., and de Boer, P. A. (2007) The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 63, 1008-1025
    • (2007) Mol. Microbiol , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.5
  • 11
    • 84877996484 scopus 로고    scopus 로고
    • The rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in escherichia coli
    • Ranjit, D. K., and Young, K. D. (2013) The Rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in Escherichia coli. J. Bacteriol. 195, 2452-2462
    • (2013) J. Bacteriol. , vol.195 , pp. 2452-2462
    • Ranjit, D.K.1    Young, K.D.2
  • 12
    • 33645021327 scopus 로고    scopus 로고
    • RF cloning: A restriction-free method for inserting target genes into plasmids
    • van den Ent, F., and Löwe, J. (2006) RF cloning: a restriction-free method for inserting target genes into plasmids. J. Biochem. Biophys. Methods 67, 67-74
    • (2006) J. Biochem. Biophys. Methods , vol.67 , pp. 67-74
    • Van Den Ent, F.1    Löwe, J.2
  • 13
    • 84879039357 scopus 로고    scopus 로고
    • (Bergfors, T. M., ed) 2nd Ed.,International University Line, La Jolla, CA
    • Larsson, A. M. (2009) in Protein Crystallization (Bergfors, T. M., ed) 2nd Ed., pp. 137-154, International University Line, La Jolla, CA
    • (2009) Protein Crystallization , pp. 137-154
    • Larsson, A.M.1
  • 20
  • 25
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda, S., and Tokuda, H. (2011) Lipoprotein sorting in bacteria. Annu. Rev. Microbiol. 65, 239-259
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 26
  • 28
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337, 635-645
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 29
    • 84864437069 scopus 로고    scopus 로고
    • DSP: A protein shape string and its profile prediction server
    • Sun, J., Tang, S., Xiong, W., Cong, P., and Li, T. (2012) DSP: a protein shape string and its profile prediction server. Nucleic Acids Res. 40, W298-302
    • (2012) Nucleic Acids Res. , vol.40
    • Sun, J.1    Tang, S.2    Xiong, W.3    Cong, P.4    Li, T.5
  • 30
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1, 2876-2890
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 32
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S -adenosylmethionine
    • Djordjevic, S., and Stock, A. M. (1997) Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S -adenosylmethionine. Structure 5, 545-558
    • (1997) Structure , vol.5 , pp. 545-558
    • Djordjevic, S.1    Stock, A.M.2
  • 33
    • 2442631494 scopus 로고    scopus 로고
    • Solution structure and domain architecture of the divisome protein FtsN
    • Yang, J. C., Van Den Ent, F., Neuhaus, D., Brevier, J., and Löwe, J. (2004) Solution structure and domain architecture of the divisome protein FtsN. Mol. Microbiol. 52, 651-660
    • (2004) Mol. Microbiol. , vol.52 , pp. 651-660
    • Yang, J.C.1    Van Den Ent, F.2    Neuhaus, D.3    Brevier, J.4    Löwe, J.5
  • 34
    • 33749427048 scopus 로고    scopus 로고
    • Balls and chains: A mesoscopic approach to tethered protein domains
    • Windisch, B., Bray, D., Duke, T. (2006) Balls and chains: a mesoscopic approach to tethered protein domains. Biophys. J. 91, 2383-2392
    • (2006) Biophys. J. , vol.91 , pp. 2383-2392
    • Windisch, B.1    Bray, D.2    Duke, T.3
  • 35
    • 62649147958 scopus 로고    scopus 로고
    • Biochemistry on a leash: The roles of tether length and geometry in signal integration proteins
    • Van Valen, D., Haataja, M., and Phillips, R. (2009) Biochemistry on a leash: the roles of tether length and geometry in signal integration proteins. Biophys. J. 96, 1275-1292
    • (2009) Biophys. J. , vol.96 , pp. 1275-1292
    • Van Valen, D.1    Haataja, M.2    Phillips, R.3
  • 38
    • 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
  • 39
    • 77954288774 scopus 로고    scopus 로고
    • Dali Server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali Server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 42
    • 84876043827 scopus 로고    scopus 로고
    • Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT
    • Terashima, H., Li, N., Sakuma, M., Koike, M., Kojima, S., Homma, M., and Imada, K. (2013) Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT. Proc. Natl. Acad. Sci. U. S. A. 110, 6133-6138
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 6133-6138
    • Terashima, H.1    Li, N.2    Sakuma, M.3    Koike, M.4    Kojima, S.5    Homma, M.6    Imada, K.7
  • 44
    • 79959976719 scopus 로고    scopus 로고
    • E. Coli histidine triad nucleotide binding protein 1 (ecHinT) is a catalytic regulator of D-alanine dehydrogenase (DadA) activity in vivo
    • Bardaweel, S., Ghosh, B., Chou, T. F., Sadowsky, M. J., and Wagner, C. R. (2011) E. coli histidine triad nucleotide binding protein 1 (ecHinT) is a catalytic regulator of D-alanine dehydrogenase (DadA) activity in vivo. PLoS One 6, e20897
    • (2011) PLoS One , vol.6
    • Bardaweel, S.1    Ghosh, B.2    Chou, T.F.3    Sadowsky, M.J.4    Wagner, C.R.5
  • 45
    • 0029738191 scopus 로고    scopus 로고
    • The convergence of murein recycling research with -lactamase research
    • Park, J. T. (1996) The convergence of murein recycling research with -lactamase research. Microb. Drug Resist. 2, 105-112
    • (1996) Microb. Drug Resist. , vol.2 , pp. 105-112
    • Park, J.T.1
  • 46
    • 84870006158 scopus 로고    scopus 로고
    • Active site plasticity within the glucoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion
    • Bacik, J. P., Whitworth, G. E., Stubbs, K. A., Vocadlo, D. J., and Mark, B. L. (2012) Active site plasticity within the glucoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion. Chem. Biol. 19, 1471-1482
    • (2012) Chem. Biol. , vol.19 , pp. 1471-1482
    • Bacik, J.P.1    Whitworth, G.E.2    Stubbs, K.A.3    Vocadlo, D.J.4    Mark, B.L.5
  • 47
  • 50
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1b, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer, W., von Rechenberg, M., and Höltje, J. V. (1999) Demonstration of molecular interactions between the murein polymerase PBP1b, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274, 6726-6734
    • (1999) J. Biol. Chem. , vol.274 , pp. 6726-6734
    • Vollmer, W.1    Von Rechenberg, M.2    Höltje, J.V.3
  • 51
    • 84874644598 scopus 로고    scopus 로고
    • Cell wall elongation mode in Gram-negative bacteria is determined by peptidoglycan architecture
    • Turner, R. D., Hurd, A. F., Cadby, A., Hobbs, J. K., and Foster, S. J. (2013) Cell wall elongation mode in Gram-negative bacteria is determined by peptidoglycan architecture. Nat. Commun. 4, 1496
    • (2013) Nat. Commun. , vol.4
    • Turner, R.D.1    Hurd, A.F.2    Cadby, A.3    Hobbs, J.K.4    Foster, S.J.5


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