Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specifity

EMBO Reports

Volumn 5, Issue 5, 2004, Pages 477-483

  van Eerde, André ^a   Hamiaux, Cyril ^a   Pérez, Javier ^b   Parsot, Claude ^c   Dijkstra, Bauke W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c INSERM   (France)

Author keywords

Chaperone; Crystal structure; Shigella; Spa15; Type III secretion

Indexed keywords

CHAPERONE; DIMER; PROTEIN SPA15; SECRETORY PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENETIC CONSERVATION; HOST PATHOGEN INTERACTION; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SHIGELLA FLEXNERI; SIGNAL TRANSDUCTION; SURFACE PROPERTY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SHIGELLA FLEXNERI;

NEGIBACTERIA; SHIGELLA; SHIGELLA FLEXNERI;

EID: 2942543052     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400144     Document Type: Article

References (25)

1. Birtalan S, Ghosh P (2001) Structure of the Yersinia type III secretory system chaperone SycE. Nat Struct Biol 8: 974-978
2. Birtalan SC, Phillips RM, Ghosh P (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9: 971-980
3. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
4. Cornelis GR (2003) How Yops find their way out of Yersinia. Mol Microbiol 50: 1091-1094
5. Creasey EA et al (2003) CesT is a bivalent enteropathogenic Escherichia coli chaperone required for translocation of both Tir and Map. Mol Microbiol 47: 209-221
6. Doublié S (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276: 523-530
7. Dubuisson JM, Decamps T, Vachette P (1997) Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions. J Appl Crystallogr 30: 49-54
8. Ehrbar K, Friebel A, Miller SI, Hardt WD (2003) Role of the Salmonella Pathogenicity Island 1 (SPI-1) protein InvB in type III secretion of SopE and SopE2, two Salmonella effector proteins encoded outside of SPI-1. J Bacteriol 185: 6950-6967
9. Evdokimov AG, Tropea JE, Routzahn KM, Waugh DS (2002) Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis. Acta Crystallogr D 58: 398-406
10. Hueck CJ. (1998) Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62: 379-433
11. Lloyd SA, Norman M, Rosqvist R, Wolf-Watz H (2001) Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol Microbiol 39: 520-531
12. Luo Y et al (2001) Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nat Struct Biol 8: 1031-1036
13. McRee DE (1999) XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156-165
14. Murshudov GN, Vagin AA, Lebedev A, Wilson KS, Dodson EJ (1999) Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallogr D 55: 247-255
15. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
16. Page AL, Parsot C (2002) Chaperones of the type III secretion pathway: jacks of all trades. Mol Microbiol 46: 1-11
17. Page AL, Fromont-Racine M, Sansonetti P, Legrain P, Parsot C (2001) Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri. Mol Microbiol 42: 1133-1145
18. Page AL, Sansonetti P, Parsot C (2002) Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway. Mol Microbiol 43: 1533-1542
19. Parsot C, Hamiaux C, Page AL (2003) The various and varying roles of specific chaperones in type III secretion systems. Curr Opin Microbiol 6: 7-14
20. Ramamurthi KS, Schneewind O (2003) Substrate recognition by the Yersinia type III protein secretion machinery. Mol Microbiol 50: 1095-1102
21. Stebbins CE, Galán JE (2001) Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414: 77-81
22. Svergun D, Barberato C, Koch MHJ (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28: 768-773
23. Terwilliger TC (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr D 59: 38-44
24. Terwilliger TC, Berendzen J (1999) Automated MAD and MIR structure solution. Acta Crystallogr D 55: 849-861
25. Weeks CM, Miller R (1999) The design and implementation of SnB version 2.0. J Appl Crystallogr 32: 120-124