메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages

Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN ASCE; PROTEIN ASCG; PROTEIN PSCE; PROTEIN PSCF; PROTEIN PSCG; PROTEIN YSCE; PROTEIN YSCF; PROTEIN YSCG; UNCLASSIFIED DRUG;

EID: 79955744846     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019208     Document Type: Article
Times cited : (12)

References (45)
  • 1
    • 0003116583 scopus 로고    scopus 로고
    • Fish pathogens
    • In: Austin B, Altwegg M, Gosling PJ, Joseph SW, editors, New York, John Wiley and Sons
    • Austin B, Adams C, (1996) Fish pathogens. In: Austin B, Altwegg M, Gosling PJ, Joseph SW, editors. The Genus Aeromonas New York John Wiley and Sons pp. 197-229.
    • (1996) The Genus Aeromonas , pp. 197-229
    • Austin, B.1    Adams, C.2
  • 2
    • 43949176579 scopus 로고
    • Pathogenesis of gram-negative bacterial infections in warmwater fish
    • Thune RL, Stanley LA, Cooper K, (1993) Pathogenesis of gram-negative bacterial infections in warmwater fish. Annu Rev Fish Dis 3: 37-68.
    • (1993) Annu Rev Fish Dis , vol.3 , pp. 37-68
    • Thune, R.L.1    Stanley, L.A.2    Cooper, K.3
  • 3
    • 0011880414 scopus 로고    scopus 로고
    • Aeromonas and Plesiomonas
    • In: Sussman M, editors, San Diego, Academic Press
    • Janda JM, (2001) Aeromonas and Plesiomonas. In: Sussman M, editors. Molecular Medical Microbiology San Diego Academic Press pp. 1237-1270.
    • (2001) Molecular Medical Microbiology , pp. 1237-1270
    • Janda, J.M.1
  • 4
    • 0030964241 scopus 로고    scopus 로고
    • Exploitation of mammalian host cell functions by bacterial pathogens
    • Finlay BB, Cossart P, (1997) Exploitation of mammalian host cell functions by bacterial pathogens. Science 276: 718-725.
    • (1997) Science , vol.276 , pp. 718-725
    • Finlay, B.B.1    Cossart, P.2
  • 5
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis GR, Van Gijsegem F, (2000) Assembly and function of type III secretory systems. Annu Rev Microbiol 54: 735-774.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 735-774
    • Cornelis, G.R.1    van Gijsegem, F.2
  • 6
    • 33645976151 scopus 로고    scopus 로고
    • New structural insights into the bacterial type III secretion system
    • Yip CK, Strynadka NCJ, (2006) New structural insights into the bacterial type III secretion system. Trends Biochem Sci 31: 223-230.
    • (2006) Trends Biochem Sci , vol.31 , pp. 223-230
    • Yip, C.K.1    Strynadka, N.C.J.2
  • 7
  • 8
    • 1342323847 scopus 로고    scopus 로고
    • A type III secretion system is required for Aeromonas hydrophila AH-1 pathogenesis
    • Yu HB, Srinivasa Rao PS, Lee HC, Vilches S, Merino S, et al. (2004) A type III secretion system is required for Aeromonas hydrophila AH-1 pathogenesis. Infect Immun 72: 1248-1256.
    • (2004) Infect Immun , vol.72 , pp. 1248-1256
    • Yu, H.B.1    Srinivasa Rao, P.S.2    Lee, H.C.3    Vilches, S.4    Merino, S.5
  • 9
    • 33847239885 scopus 로고    scopus 로고
    • Characterization of extracellular proteins produced by Aeromonas hydrophila AH-1
    • Yu HB, Kaur R, Lim S, Wang XH, Leung KY, (2007) Characterization of extracellular proteins produced by Aeromonas hydrophila AH-1. Proteomics 7: 436-449.
    • (2007) Proteomics , vol.7 , pp. 436-449
    • Yu, H.B.1    Kaur, R.2    Lim, S.3    Wang, X.H.4    Leung, K.Y.5
  • 10
    • 36849042170 scopus 로고    scopus 로고
    • Aeromonas hydrophila AH-3 AexT is an ADP-ribosylating toxin secreted through the type III secretion system
    • In press
    • Vilches S, Wilhelms M, Yu HB, Leung KY, Tomás JM, et al. (2007) Aeromonas hydrophila AH-3 AexT is an ADP-ribosylating toxin secreted through the type III secretion system. Microb Pathogenesis In press.
    • (2007) Microb Pathogenesis
    • Vilches, S.1    Wilhelms, M.2    Yu, H.B.3    Leung, K.Y.4    Tomás, J.M.5
  • 11
    • 34547602271 scopus 로고    scopus 로고
    • Further characterization of a type III secretion system (T3SS) and of a new effector protein from a clinical isolate of Aeromonas hydrophila - Part I
    • Sha J, Wang SF, Suarez G, Sierra JC, Fadl AA, et al. (2007) Further characterization of a type III secretion system (T3SS) and of a new effector protein from a clinical isolate of Aeromonas hydrophila- Part I. Microb Pathog 43: 127-146.
    • (2007) Microb Pathog , vol.43 , pp. 127-146
    • Sha, J.1    Wang, S.F.2    Suarez, G.3    Sierra, J.C.4    Fadl, A.A.5
  • 12
    • 34547600796 scopus 로고    scopus 로고
    • Biological characterization of a new type III secretion system effector from a clinical isolate of Aeromonas hydrophila - Part II
    • In press
    • Sierra JC, Suarez G, Sha J, Foltz SM, Popov VL, et al. (2007) Biological characterization of a new type III secretion system effector from a clinical isolate of Aeromonas hydrophila- Part II. Microb Pathogenesis In press.
    • (2007) Microb Pathogenesis
    • Sierra, J.C.1    Suarez, G.2    Sha, J.3    Foltz, S.M.4    Popov, V.L.5
  • 13
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan SC, Phillips RM, Ghosh P, (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9: 971-980.
    • (2002) Mol Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 14
    • 27744509836 scopus 로고    scopus 로고
    • The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa
    • Quinaud M, Chabert J, Faudry E, Neumann E, Lemaire D, et al. (2005) The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa. J Biol Chem 280: 36293-36300.
    • (2005) J Biol Chem , vol.280 , pp. 36293-36300
    • Quinaud, M.1    Chabert, J.2    Faudry, E.3    Neumann, E.4    Lemaire, D.5
  • 15
    • 33645093201 scopus 로고    scopus 로고
    • Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion
    • Edqvist PJ, Bröms JE, Betts HJ, Forsberg Å, Pallen MJ, et al. (2006) Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion. Mol Microbiol 59: 31-44.
    • (2006) Mol Microbiol , vol.59 , pp. 31-44
    • Edqvist, P.J.1    Bröms, J.E.2    Betts, H.J.3    Forsberg, Å.4    Pallen, M.J.5
  • 16
    • 37349055354 scopus 로고    scopus 로고
    • Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD
    • Büttner CR, Sorg I, Cornelis GR, Heinz DW, Niemann HH, (2008) Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD. J Mol Biol 375: 997-1012.
    • (2008) J Mol Biol , vol.375 , pp. 997-1012
    • Büttner, C.R.1    Sorg, I.2    Cornelis, G.R.3    Heinz, D.W.4    Niemann, H.H.5
  • 17
    • 77954407664 scopus 로고    scopus 로고
    • Structural basis of chaperone recognition of type III secretion system minor translocator proteins
    • Job V, Matteï P-J, Lemaire D, Attree I, Dessen A, (2010) Structural basis of chaperone recognition of type III secretion system minor translocator proteins. J Biol Chem 285: 23224-23232.
    • (2010) J Biol Chem , vol.285 , pp. 23224-23232
    • Job, V.1    Matteï, P.-J.2    Lemaire, D.3    Attree, I.4    Dessen, A.5
  • 18
    • 52949139839 scopus 로고    scopus 로고
    • Structure of AscE and induced burial regions in AscE and AscG upon formation of the chaperone needle-subunit complex of type III secretion system in Aeromonas hydrophila
    • Tan YW, Yu HB, Leung KY, Sivaraman J, Mok Y-K, (2008) Structure of AscE and induced burial regions in AscE and AscG upon formation of the chaperone needle-subunit complex of type III secretion system in Aeromonas hydrophila. Protein Sci 17: 1748-1760.
    • (2008) Protein Sci , vol.17 , pp. 1748-1760
    • Tan, Y.W.1    Yu, H.B.2    Leung, K.Y.3    Sivaraman, J.4    Mok, Y.-K.5
  • 19
    • 25844498470 scopus 로고    scopus 로고
    • Crystal structure of the Yersinia type III secretion protein YscE
    • Phan J, Austin BP, Waugh DS, (2005) Crystal structure of the Yersinia type III secretion protein YscE. Protein Sci 14: 2759-2763.
    • (2005) Protein Sci , vol.14 , pp. 2759-2763
    • Phan, J.1    Austin, B.P.2    Waugh, D.S.3
  • 20
    • 40649128950 scopus 로고    scopus 로고
    • Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG
    • Sun P, Tropea JE, Austin BP, Cherry S, Waugh DS, (2008) Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG. J Mol Biol 377: 819-830.
    • (2008) J Mol Biol , vol.377 , pp. 819-830
    • Sun, P.1    Tropea, J.E.2    Austin, B.P.3    Cherry, S.4    Waugh, D.S.5
  • 21
    • 34249942920 scopus 로고    scopus 로고
    • Structure of the heterotrimetric complex that regulates type III secretion needle formation
    • Quinaud M, Plé S, Job V, Contreras-Martel C, Simorre J-P, et al. (2007) Structure of the heterotrimetric complex that regulates type III secretion needle formation. Proc Natl Acad Sci USA 104: 7803-7808.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7803-7808
    • Quinaud, M.1    Plé, S.2    Job, V.3    Contreras-Martel, C.4    Simorre, J.-P.5
  • 22
    • 51049124329 scopus 로고    scopus 로고
    • The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE
    • Rodgers L, Gamez A, Riek R, Ghosh P, (2008) The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. J Biol Chem 283: 20857-20863.
    • (2008) J Biol Chem , vol.283 , pp. 20857-20863
    • Rodgers, L.1    Gamez, A.2    Riek, R.3    Ghosh, P.4
  • 23
    • 67749106086 scopus 로고    scopus 로고
    • Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila
    • Tan YW, Yu HB, Sivaraman J, Leung KY, Mok Y-K, (2009) Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila. Protein Sci 18: 1724-1734.
    • (2009) Protein Sci , vol.18 , pp. 1724-1734
    • Tan, Y.W.1    Yu, H.B.2    Sivaraman, J.3    Leung, K.Y.4    Mok, Y.-K.5
  • 24
    • 40749148575 scopus 로고    scopus 로고
    • On distance and similarity in fold space
    • Sippl MJ, (2008) On distance and similarity in fold space. Bioinformatics 24: 872-873.
    • (2008) Bioinformatics , vol.24 , pp. 872-873
    • Sippl, M.J.1
  • 25
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • Sippl MJ, Wiederstein M, (2008) A note on difficult structure alignment problems. Bioinformatics 24: 426-427.
    • (2008) Bioinformatics , vol.24 , pp. 426-427
    • Sippl, M.J.1    Wiederstein, M.2
  • 26
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, 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
  • 27
    • 0028904072 scopus 로고
    • Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)
    • Ruiz-Sanz J, de Prat Gay G, Otzen DE, Fersht AR, (1995) Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2). Biochemistry 34: 1695-1701.
    • (1995) Biochemistry , vol.34 , pp. 1695-1701
    • Ruiz-Sanz, J.1    de Prat Gay, G.2    Otzen, D.E.3    Fersht, A.R.4
  • 28
    • 0034753703 scopus 로고    scopus 로고
    • Structure of the Yersinia type III secretory system chaperone SycE
    • Birtalan S, Ghosh P, (2001) Structure of the Yersinia type III secretory system chaperone SycE. Nat Struct Mol Biol 8: 974-978.
    • (2001) Nat Struct Mol Biol , vol.8 , pp. 974-978
    • Birtalan, S.1    Ghosh, P.2
  • 29
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type III secretion translocator
    • Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M, (2009) IpaB-IpgC interaction defines binding motif for type III secretion translocator. Proc Natl Acad Sci USA 106: 9661-9666.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 30
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL, (2005) Natively unfolded proteins. Curr Opin Struct Biol 15: 35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 31
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE, (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 32
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P, Csermely P, (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J 18: 1169-1175.
    • (2004) FASEB J , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 33
    • 0037472730 scopus 로고    scopus 로고
    • Interaction of the disordered terminal regions of flagellin upon flagellar filament formation
    • Gugolya Z, Muskotal A, Sebestyen A, Dioszeghy Z, Vonderviszt F, (2003) Interaction of the disordered terminal regions of flagellin upon flagellar filament formation. FEBS Lett 535: 66-70.
    • (2003) FEBS Lett , vol.535 , pp. 66-70
    • Gugolya, Z.1    Muskotal, A.2    Sebestyen, A.3    Dioszeghy, Z.4    Vonderviszt, F.5
  • 34
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis JM, Johansson K, Receveur-Brechot V, Oldfield CJ, Dunker KA, et al. (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 99: 157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5
  • 35
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface for phasing with SHELX programs
    • Pape T, Schneider TR, (2004) HKL2MAP: a graphical user interface for phasing with SHELX programs. J Appl Cryst 37: 843-844.
    • (2004) J Appl Cryst , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 36
    • 0042810719 scopus 로고    scopus 로고
    • Towards automated protein structure determination: BnP, the SnB-PHASES interface
    • Weeks CM, Blessing RH, Miller R, Mungee R, Potter SA, et al. (2002) Towards automated protein structure determination: BnP, the SnB-PHASES interface. Z Kristallogr 217: 686-693.
    • (2002) Z Kristallogr , vol.217 , pp. 686-693
    • Weeks, C.M.1    Blessing, R.H.2    Miller, R.3    Mungee, R.4    Potter, S.A.5
  • 37
    • 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 Cryst D Biol Crystallogr D50: 760-763.
    • (1994) Acta Cryst D Biol Crystallogr , vol.D50 , pp. 760-763
  • 38
    • 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. Nature Protocols 3: 1171-1179.
    • (2008) Nature Protocols , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Cryst D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Cryst D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M, (1991) Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Cryst A47: 110-119.
    • (1991) Acta Cryst , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 41
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Cryst D Biol Crystallogr 54: 905-921.
    • (1998) Acta Cryst D Biol Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 45
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • DeLano Scientific, Palo Alto, CA, USA
    • DeLano WL, (2002) The PyMOL molecular graphics system. DeLano Scientific, Palo Alto, CA, USAhttp://www.pymol.org.
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.