Structural characterization of the molecular platform for type III secretion system assembly

Nature

Volumn 435, Issue 7042, 2005, Pages 702-707

  Yip, Calvin K ^a   Kimbrough, Tyler G ^b   Felise, Heather B ^c   Vuckovic, Marija ^a   Thomas, Nikhil A ^d   Pfuetzner, Richard A ^a   Frey, Elizabeth A ^a   Finlay, B Brett ^d   Miller, Samuel I ^b,c   Strynadka, Natalie C J ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY OF WASHINGTON   (United States)

^c Box 357710 ^*  (United States)

^d UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ESCHERICHIA COLI; MASS SPECTROMETRY; MORPHOLOGY; PATHOLOGY; STOICHIOMETRY; STRUCTURE (COMPOSITION); VIRUSES;

CRYSTAL PACKING ANALYSIS; GRAM-NEGATIVE PATHOGENS; MOLECULAR MODELING; SECRETION SYSTEMS;

PROTEINS;

BACTERIAL PROTEIN; ESCJ PROTEIN; PRGK PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; YSCJ PROTEIN; ESCHERICHIA COLI PROTEIN;

MEDICINE;

ARTICLE; BACTERIAL MEMBRANE; BACTERIAL VIRULENCE; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ENTEROPATHOGENIC ESCHERICHIA COLI; ESCHERICHIA COLI; EUKARYOTIC CELL; FLAGELLUM; GENETIC CONSERVATION; GRAM NEGATIVE BACTERIUM; MACROMOLECULE; MASS SPECTROMETRY; MEMBRANE BINDING; MOLECULAR MODEL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SALMONELLA TYPHIMURIUM; SALMONELLA TYPHIMURIUM PRGK; STOICHIOMETRY; STRUCTURE ANALYSIS; TYPE III SECRETION SYSTEM; AMINO ACID SEQUENCE; BIOTINYLATION; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ELECTRICITY; ENTROPY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SECRETION; X RAY CRYSTALLOGRAPHY;

ANIMALIA; ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA; SALMONELLA TYPHIMURIUM;

AMINO ACID SEQUENCE; BIOTINYLATION; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENTROPY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN TRANSPORT; SALMONELLA TYPHIMURIUM; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 20444488138     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03554     Document Type: Article

References (28)

1. Ghosh, P. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68, 771-795 (2004).
2. Marlovits, T. C. et al. Structural insights into the assembly of the type III secretion needle complex. Science 306, 1040-1042 (2004).
3. Kubori, T. et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280, 602-605 (1998)
4. Blocker, A. et al. Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton. Mol. Microbiol. 39, 652-663 (2001).
5. Kimbrough, T. G. & Miller, S. I. Assembly of the type III secretion needle complex of Salmonella typhimurium. Microbes Infect. 4, 75-82 (2002).
6. Kimbrough, T. G. & Miller, S. I. Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc. Natl Acad. Sci. USA 97, 11008-11013 (2000).
7. Galan, J. E. & Collmer, A. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284, 1322-1328 (1999).
8. Sukhan, A., Kubori, T., Wilson, J. & Galan, J. E. Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J. Bacteriol. 183, 1159-1167 (2001).
9. Crago, A. M. & Koronakis, V. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30, 47-56 (1998).
10. Aizawa, S. I. Flagellar assembly in Salmonella typhimurium. Mol. Microbiol. 19, 1-5 (1996).
11. Burghout, P. et al. Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica. J. Bacteriol. 186, 4645-4654 (2004).
12. Linderoth, N. A., Simon, M. N. & Russel, M. The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 278, 1635-1638 (1997).
13. Nouwen, N. et al. Secretin PuID: association with pilot PuIS, structure, and ion-conducting channel formation, Proc Natl Acad. Sci. USA 96, 8173-8177 (1999).
14. Jones, C. J., Macnab, R. M., Okino, H. & Aizawa, S. Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium. J. Mol. Biol. 212, 377-387 (1990).
15. Sekiya, K. et al. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl Acad. Sci. USA 98, 11638-11643 (2001).
16. Suzuki, H., Yonekura, K. & Namba, K. Structure of the rotor of the bacterial ftagellar motor reveated by electron cryomicroscopy and single-particle image analysis, J. Mol. Biol. 337, 105-113 (2004).
17. Thomas, J., Stafford, G. P. & Hughes, C. Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc. Natl Acad. Sci. USA 101, 3945-3950 (2004).
18. Leslie, A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsl. Protein Crystollogr. no. 26 (1992).
19. Evans, P. R. Data reduction, Proc. CCP4 Study Weekend on Data Collection and Processing 114-122, (1993).
20. Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystollogr. D 55, 849-861 (1999).
21. Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
22. McRee, D. E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165 (1999).
23. Erunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
24. Murshudov, G. N. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
25. Kabsch, W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32, 922-923 (1976).
26. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
27. Kraulis, P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl Crystallogr. 24, 946-950 (1991).
28. Merritt, E. A. B. & Bacon, D. J. Raster3D: photorealistic Molecular Graphics. Methods Enzymol. 277, 505-524 (1997).