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Volumn 21, Issue 5, 2013, Pages 741-752

Structural insight into the giant Ca2+-binding adhesin siie: Implications for the adhesion of salmonella enterica to polarized epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; BACTERIUM LIPOPOLYSACCHARIDE; CALCIUM BINDING PROTEIN;

EID: 84877576585     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.02.020     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • DATABASE ISSUE
    • H. Berman, K. Henrick, H. Nakamura, and J.L. Markley The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data Nucleic Acids Res. 35 Database issue 2007 D301 D303
    • (2007) Nucleic Acids Res. , vol.35
    • Berman, H.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 33646192726 scopus 로고    scopus 로고
    • Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants
    • S. Cook, T.E. Schäffer, K.M. Chynoweth, M. Wigton, R.W. Simmonds, and K.M. Lang Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants Nanotechnology 17 2006 2135 2145
    • (2006) Nanotechnology , vol.17 , pp. 2135-2145
    • Cook, S.1    Schäffer, T.E.2    Chynoweth, K.M.3    Wigton, M.4    Simmonds, R.W.5    Lang, K.M.6
  • 9
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: Crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • C.C. Deivanayagam, E.R. Wann, W. Chen, M. Carson, K.R. Rajashankar, M. Höök, and S.V. Narayana A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A EMBO J. 21 2002 6660 6672
    • (2002) EMBO J. , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5    Höök, M.6    Narayana, S.V.7
  • 10
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • R. Dutzler, Y.F. Wang, P. Rizkallah, J.P. Rosenbusch, and T. Schirmer Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway Structure 4 1996 127 134
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 11
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 13
    • 0029901637 scopus 로고    scopus 로고
    • Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods
    • J. Felsenstein Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods Methods Enzymol. 266 1996 418 427
    • (1996) Methods Enzymol. , vol.266 , pp. 418-427
    • Felsenstein, J.1
  • 14
    • 34250739997 scopus 로고    scopus 로고
    • Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system
    • R.G. Gerlach, D. Jäckel, B. Stecher, C. Wagner, A. Lupas, W.D. Hardt, and M. Hensel Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system Cell. Microbiol. 9 2007 1834 1850
    • (2007) Cell. Microbiol. , vol.9 , pp. 1834-1850
    • Gerlach, R.G.1    Jäckel, D.2    Stecher, B.3    Wagner, C.4    Lupas, A.5    Hardt, W.D.6    Hensel, M.7
  • 15
    • 54049111835 scopus 로고    scopus 로고
    • Cooperation of Salmonella pathogenicity islands 1 and 4 is required to breach epithelial barriers
    • R.G. Gerlach, N. Cláudio, M. Rohde, D. Jäckel, C. Wagner, and M. Hensel Cooperation of Salmonella pathogenicity islands 1 and 4 is required to breach epithelial barriers Cell. Microbiol. 10 2008 2364 2376
    • (2008) Cell. Microbiol. , vol.10 , pp. 2364-2376
    • Gerlach, R.G.1    Cláudio, N.2    Rohde, M.3    Jäckel, D.4    Wagner, C.5    Hensel, M.6
  • 16
    • 33744502092 scopus 로고    scopus 로고
    • Small revisions to predicted distances around metal sites in proteins
    • M.M. Harding Small revisions to predicted distances around metal sites in proteins Acta Crystallogr. D Biol. Crystallogr. 62 2006 678 682
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 678-682
    • Harding, M.M.1
  • 17
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • WEB SERVER ISSUE W545-9
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 Web Server issue 2010 W545-9
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 18
    • 84855500089 scopus 로고    scopus 로고
    • Microbial adhesins to gastrointestinal mucus
    • N. Juge Microbial adhesins to gastrointestinal mucus Trends Microbiol. 20 2012 30 39
    • (2012) Trends Microbiol. , vol.20 , pp. 30-39
    • Juge, N.1
  • 19
    • 0034780639 scopus 로고    scopus 로고
    • Interaction of bacterial pathogens with polarized epithelium
    • B.I. Kazmierczak, K. Mostov, and J.N. Engel Interaction of bacterial pathogens with polarized epithelium Annu. Rev. Microbiol. 55 2001 407 435
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 407-435
    • Kazmierczak, B.I.1    Mostov, K.2    Engel, J.N.3
  • 20
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 28244447376 scopus 로고    scopus 로고
    • BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis
    • C. Latasa, A. Roux, A. Toledo-Arana, J.M. Ghigo, C. Gamazo, J.R. Penadés, and I. Lasa BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis Mol. Microbiol. 58 2005 1322 1339
    • (2005) Mol. Microbiol. , vol.58 , pp. 1322-1339
    • Latasa, C.1    Roux, A.2    Toledo-Arana, A.3    Ghigo, J.M.4    Gamazo, C.5    Penadés, J.R.6    Lasa, I.7
  • 22
    • 0016138377 scopus 로고
    • The barrier function of the gram-negative envelope
    • L. Leive The barrier function of the gram-negative envelope Ann. NY Acad. Sci. 235 1974 109 129
    • (1974) Ann. NY Acad. Sci. , vol.235 , pp. 109-129
    • Leive, L.1
  • 23
    • 77954843913 scopus 로고    scopus 로고
    • LapF, the second largest Pseudomonas putida protein, contributes to plant root colonization and determines biofilm architecture
    • M. Martínez-Gil, F. Yousef-Coronado, and M. Espinosa-Urgel LapF, the second largest Pseudomonas putida protein, contributes to plant root colonization and determines biofilm architecture Mol. Microbiol. 77 2010 549 561
    • (2010) Mol. Microbiol. , vol.77 , pp. 549-561
    • Martínez-Gil, M.1    Yousef-Coronado, F.2    Espinosa-Urgel, M.3
  • 24
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution
    • A.P. May, R.C. Robinson, M. Vinson, P.R. Crocker, and E.Y. Jones Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution Mol. Cell 1 1998 719 728
    • (1998) Mol. Cell , vol.1 , pp. 719-728
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3    Crocker, P.R.4    Jones, E.Y.5
  • 25
    • 33847750775 scopus 로고    scopus 로고
    • SiiE is secreted by the Salmonella enterica serovar Typhimurium pathogenicity island 4-encoded secretion system and contributes to intestinal colonization in cattle
    • E. Morgan, A.J. Bowen, S.C. Carnell, T.S. Wallis, and M.P. Stevens SiiE is secreted by the Salmonella enterica serovar Typhimurium pathogenicity island 4-encoded secretion system and contributes to intestinal colonization in cattle Infect. Immun. 75 2007 1524 1533
    • (2007) Infect. Immun. , vol.75 , pp. 1524-1533
    • Morgan, E.1    Bowen, A.J.2    Carnell, S.C.3    Wallis, T.S.4    Stevens, M.P.5
  • 28
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: A novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 30
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-A structural perspective
    • C.A. Orengo, and J.M. Thornton Protein families and their evolution-a structural perspective Annu. Rev. Biochem. 74 2005 867 900
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 31
    • 24044553899 scopus 로고    scopus 로고
    • Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7
    • H. Orikoshi, S. Nakayama, C. Hanato, K. Miyamoto, and H. Tsujibo Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7 J. Appl. Microbiol. 99 2005 551 557
    • (2005) J. Appl. Microbiol. , vol.99 , pp. 551-557
    • Orikoshi, H.1    Nakayama, S.2    Hanato, C.3    Miyamoto, K.4    Tsujibo, H.5
  • 35
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, M. Gautel, F. Oesterhelt, J.M. Fernandez, and H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 1109 1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 36
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • M. Rief, J. Pascual, M. Saraste, and H.E. Gaub Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles J. Mol. Biol. 286 1999 553 561
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 37
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • G.M. Sheldrick A short history of SHELX Acta Crystallogr. A 64 2008 112 122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 38
    • 80955155552 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica
    • K.U. Sturm, M.H. Griessl, C. Wagner, J. Deiwick, M. Hensel, and Y.A. Muller Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 2011 1371 1374
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 1371-1374
    • Sturm, K.U.1    Griessl, M.H.2    Wagner, C.3    Deiwick, J.4    Hensel, M.5    Muller, Y.A.6
  • 39
    • 0018852410 scopus 로고
    • Rotary shadowing of extended molecules dried from glycerol
    • J.M. Tyler, and D. Branton Rotary shadowing of extended molecules dried from glycerol J. Ultrastruct. Res. 71 1980 95 102
    • (1980) J. Ultrastruct. Res. , vol.71 , pp. 95-102
    • Tyler, J.M.1    Branton, D.2
  • 42
    • 0033915675 scopus 로고    scopus 로고
    • Ligand-binding sites in Ig-like domains of receptor tyrosine kinases
    • C. Wiesmann, Y.A. Muller, and A.M. de Vos Ligand-binding sites in Ig-like domains of receptor tyrosine kinases J. Mol. Med. 78 2000 247 260
    • (2000) J. Mol. Med. , vol.78 , pp. 247-260
    • Wiesmann, C.1    Muller, Y.A.2    De Vos, A.M.3


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