메뉴 건너뛰기




Volumn 5, Issue 9, 2010, Pages 1-9

Structure of a Burkholderia pseudomallei Trimeric Autotransporter Adhesin head

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; TRIMERIC AUTOTRANSPORTER ADHESIN; UNCLASSIFIED DRUG; ADHESIN;

EID: 77958499676     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012803     Document Type: Article
Times cited : (32)

References (49)
  • 1
    • 34047229212 scopus 로고    scopus 로고
    • Burkholderia Hep_Hag autotransporter (BuHA) proteins elicit a strong antibody response during experimental glanders but not human melioidosis
    • Tiyawisutsri R, Holden MT, Tumapa S, Rengpipat S, Clarke SR, et al. (2007) Burkholderia Hep_Hag autotransporter (BuHA) proteins elicit a strong antibody response during experimental glanders but not human melioidosis. BMC Microbiol 7: 19.
    • (2007) BMC Microbiol , vol.7 , pp. 19
    • Tiyawisutsri, R.1    Holden, M.T.2    Tumapa, S.3    Rengpipat, S.4    Clarke, S.R.5
  • 3
    • 43349091607 scopus 로고    scopus 로고
    • Domain annotation of trimeric autotransporter adhesions-daTAA
    • Szczesny P, Lupas A (2008) Domain annotation of trimeric autotransporter adhesions-daTAA. Bioinformatics 24: 1251-1256.
    • (2008) Bioinformatics , vol.24 , pp. 1251-1256
    • Szczesny, P.1    Lupas, A.2
  • 4
    • 77950678687 scopus 로고    scopus 로고
    • Genome-wide analysis of DNA repeats in Burkholderia cenocepacia J2315 identifies a novel adhesin-like gene unique to epidemic-associated strains of the ET-12 lineage
    • Mil-Homens D, Rocha EP, Fialho AM (2010) Genome-wide analysis of DNA repeats in Burkholderia cenocepacia J2315 identifies a novel adhesin-like gene unique to epidemic-associated strains of the ET-12 lineage. Microbiology 156: 1084-1096.
    • (2010) Microbiology , vol.156 , pp. 1084-1096
    • Mil-Homens, D.1    Rocha, E.P.2    Fialho, A.M.3
  • 5
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk E, Roggenkamp A, Reichenbecher M, Lupas A, Heesemann J (2000) Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J 19: 5989-5999.
    • (2000) EMBO J , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 6
    • 0033939582 scopus 로고    scopus 로고
    • Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification Of eight NSVAIG - S motifs in the amino-terminal half of the protein involved in collagen binding
    • Tahir YE, Kuusela P, Skurnik M (2000) Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification Of eight NSVAIG - S motifs in the amino-terminal half of the protein involved in collagen binding. Mol Microbiol 37: 192-206.
    • (2000) Mol Microbiol , vol.37 , pp. 192-206
    • Tahir, Y.E.1    Kuusela, P.2    Skurnik, M.3
  • 7
    • 1842562406 scopus 로고    scopus 로고
    • The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll
    • Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M, et al. (2004) The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. EMBO J 23: 701-711.
    • (2004) EMBO J , vol.23 , pp. 701-711
    • Nummelin, H.1    Merckel, M.C.2    Leo, J.C.3    Lankinen, H.4    Skurnik, M.5
  • 8
    • 47649089793 scopus 로고    scopus 로고
    • The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity
    • Leo JC, Elovaara H, Brodsky B, Skurnik M, Goldman A (2008) The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity. Protein Eng Des Sel 21: 475-484.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 475-484
    • Leo, J.C.1    Elovaara, H.2    Brodsky, B.3    Skurnik, M.4    Goldman, A.5
  • 9
    • 56249146661 scopus 로고    scopus 로고
    • Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng G, St Geme JW, 3rd, Waksman G (2008) Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter. J Mol Biol 384: 824-836.
    • (2008) J Mol Biol , vol.384 , pp. 824-836
    • Meng, G.1    St Geme III, J.W.2    Waksman, G.3
  • 10
    • 1942535748 scopus 로고    scopus 로고
    • Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter
    • Yeo HJ, Cotter SE, Laarmann S, Juehne T, St Geme JW, 3rd, et al. (2004) Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter. EMBO J 23: 1245-1256.
    • (2004) EMBO J , vol.23 , pp. 1245-1256
    • Yeo, H.J.1    Cotter, S.E.2    Laarmann, S.3    Juehne, T.4    St Geme III, J.W.5
  • 12
    • 77951974279 scopus 로고    scopus 로고
    • A transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled-coil segment of trimeric autotransporter adhesins
    • Alvarez BH, Gruber M, Ursinus A, Dunin-Horkawicz S, Lupas AN, et al. (2010) A transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled-coil segment of trimeric autotransporter adhesins. J Struct Biol 170: 236-245.
    • (2010) J Struct Biol , vol.170 , pp. 236-245
    • Alvarez, B.H.1    Gruber, M.2    Ursinus, A.3    Dunin-Horkawicz, S.4    Lupas, A.N.5
  • 14
    • 47049122542 scopus 로고    scopus 로고
    • The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil
    • Conners R, Hill DJ, Borodina E, Agnew C, Daniell SJ, et al. (2008) The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil. EMBO J 27: 1779-1789.
    • (2008) EMBO J , vol.27 , pp. 1779-1789
    • Conners, R.1    Hill, D.J.2    Borodina, E.3    Agnew, C.4    Daniell, S.J.5
  • 15
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng G, Surana NK, St Geme JW, 3rd, Waksman G (2006) Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J 25: 2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St Geme III, J.W.3    Waksman, G.4
  • 16
    • 77949323924 scopus 로고    scopus 로고
    • Crystal structure of a full-length autotransporter
    • van den Berg B (2010) Crystal structure of a full-length autotransporter. J Mol Biol 396: 627-633.
    • (2010) J Mol Biol , vol.396 , pp. 627-633
    • van den Berg, B.1
  • 17
    • 70350517632 scopus 로고    scopus 로고
    • Genomics of emerging infectious disease: A PLoS collection
    • Eisen JA, MacCallum CJ (2009) Genomics of emerging infectious disease: A PLoS collection. PLoS Biol 7: e1000224.
    • (2009) PLoS Biol , vol.7
    • Eisen, J.A.1    Maccallum, C.J.2
  • 19
    • 70350479576 scopus 로고    scopus 로고
    • The key role of genomics in modern vaccine and drug design for emerging infectious diseases
    • Seib KL, Dougan G, Rappuoli R (2009) The key role of genomics in modern vaccine and drug design for emerging infectious diseases. PLoS Genet 5: e1000612.
    • (2009) PLoS Genet , vol.5
    • Seib, K.L.1    Dougan, G.2    Rappuoli, R.3
  • 20
    • 70350479575 scopus 로고    scopus 로고
    • The role of medical structural genomics in discovering new drugs for infectious diseases
    • Van Voorhis WC, Hol WG, Myler PJ, Stewart LJ (2009) The role of medical structural genomics in discovering new drugs for infectious diseases. PLoS Comput Biol 5: e1000530.
    • (2009) PLoS Comput Biol , vol.5
    • van Voorhis, W.C.1    Hol, W.G.2    Myler, P.J.3    Stewart, L.J.4
  • 21
    • 0036437046 scopus 로고    scopus 로고
    • A high-molecular-weight outer membrane protein of Xanthomonas oryzae pv. oryzae exhibits similarity to non-fimbrial adhesins of animal pathogenic bacteria and is required for optimum virulence
    • Ray SK, Rajeshwari R, Sharma Y, Sonti RV (2002) A high-molecular-weight outer membrane protein of Xanthomonas oryzae pv. oryzae exhibits similarity to non-fimbrial adhesins of animal pathogenic bacteria and is required for optimum virulence. Mol Microbiol 46: 637-647.
    • (2002) Mol Microbiol , vol.46 , pp. 637-647
    • Ray, S.K.1    Rajeshwari, R.2    Sharma, Y.3    Sonti, R.V.4
  • 24
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar RC (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 25
    • 30344438515 scopus 로고    scopus 로고
    • Automated prediction of domain boundaries in CASP6 targets using Ginzu and RosettaDOM
    • Kim DE, Chivian D, Malmstrom L, Baker D (2005) Automated prediction of domain boundaries in CASP6 targets using Ginzu and RosettaDOM. Proteins 61 Suppl 7: 193-200.
    • (2005) Proteins 61 Suppl , vol.7 , pp. 193-200
    • Kim, D.E.1    Chivian, D.2    Malmstrom, L.3    Baker, D.4
  • 27
    • 32944460868 scopus 로고    scopus 로고
    • Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: The PACT/JCSG+ strategy
    • Newman J, Egan D, Walter TS, Meged R, Berry I, et al. (2005) Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy. Acta Crystallogr D Biol Crystallogr 61: 1426-1431.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 1426-1431
    • Newman, J.1    Egan, D.2    Walter, T.S.3    Meged, R.4    Berry, I.5
  • 28
    • 64549153594 scopus 로고    scopus 로고
    • In situ proteolysis to generate crystals for structure determination: An update
    • Wernimont A, Edwards A (2009) In situ proteolysis to generate crystals for structure determination: an update. PLoS One 4: e5094.
    • (2009) PLoS One , vol.4
    • Wernimont, A.1    Edwards, A.2
  • 29
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff KA, Rupp B (2003) Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. Protein Sci 12: 1865-1871.
    • (2003) Protein Sci , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 30
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (1968) Solvent content of protein crystals. JMol Biol 33: 491-497.
    • (1968) JMol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 31
    • 36549040856 scopus 로고    scopus 로고
    • Phase determination using halide ions
    • Dauter M, Dauter Z (2007) Phase determination using halide ions. Methods Mol Biol 364: 149-158.
    • (2007) Methods Mol Biol , vol.364 , pp. 149-158
    • Dauter, M.1    Dauter, Z.2
  • 32
    • 34447623057 scopus 로고    scopus 로고
    • SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: Effects of data redundancy and completeness on structure solution
    • Yogavel M, Gill J, Mishra PC, Sharma A (2007) SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution. Acta Crystallogr D Biol Crystallogr 63: 931-934.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 931-934
    • Yogavel, M.1    Gill, J.2    Mishra, P.C.3    Sharma, A.4
  • 33
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 34
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • Mason JM, Arndt KM (2004) Coiled coil domains: stability, specificity, and biological implications. Chembiochem 5: 170-176.
    • (2004) Chembiochem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 36
    • 77952793285 scopus 로고    scopus 로고
    • Evolution of outer membrane beta-barrels from an ancestral beta beta hairpin
    • Remmert M, Biegert A, Linke D, Lupas AN, Soding J (2010) Evolution of outer membrane beta-barrels from an ancestral beta beta hairpin. Mol Biol Evol 27: 1348-1358.
    • (2010) Mol Biol Evol , vol.27 , pp. 1348-1358
    • Remmert, M.1    Biegert, A.2    Linke, D.3    Lupas, A.N.4    Soding, J.5
  • 37
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher T, Helmann JD, Unden G (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 70: 910-938.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 38
    • 77954384425 scopus 로고    scopus 로고
    • Structural characterization of the predominant family of histidine kinase sensor domains
    • Zhang Z, Hendrickson WA (2010) Structural characterization of the predominant family of histidine kinase sensor domains. JMol Biol 400: 335-353.
    • (2010) JMol Biol , vol.400 , pp. 335-353
    • Zhang, Z.1    Hendrickson, W.A.2
  • 39
    • 67651244131 scopus 로고    scopus 로고
    • Siderocalins: Siderophore-binding proteins of the innate immune system
    • Clifton MC, Corrent C, Strong RK (2009) Siderocalins: siderophore-binding proteins of the innate immune system. Biometals 22: 557-564.
    • (2009) Biometals , vol.22 , pp. 557-564
    • Clifton, M.C.1    Corrent, C.2    Strong, R.K.3
  • 40
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C, de Jong PJ (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18: 6069-6074.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 41
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 42
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor W, Cymborowski M, Otwinowski Z, Chruszcz M (2006) HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr D Biol Crystallogr 62: 859-866.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 46
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr D Biol Crystallogr 62: 1002-1011.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 47
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3: 1171-1179.
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 49


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.