Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei

Journal of Molecular Biology

Volumn 359, Issue 2, 2006, Pages 322-330

  Zhang, Lingling ^a   Wang, Yu ^a   Picking, Wendy L ^a   Picking, William D ^a   De Guzman, Roberto N ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

BsaL; needle protein; NMR; pathogenesis; type III secretion

Indexed keywords

BACTERIAL PROTEIN; BSA L PROTEIN; HELIX LOOP HELIX PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BURKHOLDERIA PSEUDOMALLEI; GRAM NEGATIVE BACTERIUM; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN SECRETION; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); BURKHOLDERIA PSEUDOMALLEI; NEGIBACTERIA;

EID: 33646180623     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.03.028     Document Type: Article

References (37)

1. Hueck C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62 (1998) 379-433
2. Kolavic S.A., Kimura A., Simons S.L., Slutsker L., Barth S., and Haley C.E. An outbreak of Shigella dysenteriae type 2 among laboratory workers due to intentional food contamination. JAMA 278 (1997) 396-398
3. Torok T.J., Tauxe R.V., Wise R.P., Livengood J.R., Sokolow R., Mauvais S., et al. A large community outbreak of salmonellosis caused by intentional contamination of restaurant salad bars. JAMA 278 (1997) 389-395
4. Dance D.A. Melioidosis: the tip of the iceberg?. Clin. Microbiol. Rev. 4 (1991) 52-60
5. Currie B.J., Fisher D.A., Howard D.M., and Burrow J.N. Neurological melioidosis. Acta Trop. 74 (2000) 145-151
6. Dance D.A. Melioidosis as an emerging global problem. Acta Trop. 74 (2000) 115-119
7. Chaowagul W., Suputtamongkol Y., Dance D.A., Rajchanuvong A., Pattara-arechachai J., and White N.J. Relapse in melioidosis: incidence and risk factors. J. Infect. Dis. 168 (1993) 1181-1185
8. Stevens M.P., Wood M.W., Taylor L.A., Monaghan P., Hawes P., Jones P.W., et al. An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen. Mol. Microbiol. 46 (2002) 649-659
9. Jones A.L., Beveridge T.J., and Woods D.E. Intracellular survival of Burkholderia pseudomallei. Infect. Immun. 64 (1996) 782-790
10. Blocker A., Komoriya K., and Aizawa S. Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc. Natl Acad. Sci. USA 100 (2003) 3027-3030
11. Cordes F.S., Komoriya K., Larquet E., Yang S., Egelman E.H., and Blocker A. Helical structure of the needle of the type III secretion system of Shigella flexneri. J. Biol. Chem. 278 (2003) 17103-17107
12. Marlovits T.C., Kubori T., Sukhan A., Thomas D.R., Galan J.E., and Unger V.M. Structural insights into the assembly of the type III secretion needle complex. Science 306 (2004) 1040-1042
13. Journet L., Agrain C., Broz P., and Cornelis G.R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302 (2003) 1757-1760
14. Pastor A., Chabert J., Louwagie M., Garin J., and Attree I. PscF is a major component of the Pseudomonas aeruginosa type III secretion needle. FEMS Microbiol. Letters 253 (2005) 95-101
15. Cordes F.S., Daniell S., Kenjale R., Saurya S., Picking W.L., Picking W.D., et al. Helical packing of needles from functionally altered Shigella type III secretion systems. J. Mol. Biol. 354 (2005) 206-211
16. Kenjale R., Wilson J., Zenk S.F., Saurya S., Picking W.L., Picking W.D., and Blocker A. The needle component of the type III secreton of Shigella regulates the activity of the secretion apparatus. J. Biol. Chem. 280 (2005) 42929-42937
17. Torruellas J., Jackson M.W., Pennock J.W., and Plano G.V. The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion. Mol. Microbiol. 57 (2005) 1719-1733
18. Darboe N., Kenjale R., Picking W.L., Picking W.D., and Middaugh C.R. Physical characterization of MxiH and PrgI, the needle component of the type III secretion apparatus from Shigella and Salmonella. Protein Sci. 15 (2006) 543-552
19. Quinaud M., Chabert J., Faudry E., Neumann E., Lemaire D., Pastor A., et al. The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa. J. Biol. Chem. 280 (2005) 36293-36300
20. 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry 31 (1992) 8180-8190
21. Muhandiram D.R., and Kay L.E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. ser. B 103 (1994) 203-216
22. Fesik S.W., and Zuiderweg E.R.P. Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 78 (1998) 588-593
23. 15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry 28 (1989) 6150-6156
24. Wishart D.S., and Nip A.M. Protein chemical shift analysis: a practical guide. Biochem. Cell Biol. 76 (1998) 153-163
25. Wuthrich K. NMR of Proteins and Nucleic Acids (1986), Wiley-Interscience, New York, NY
26. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
27. Phan J., Austin B.P., and Waugh D.S. Crystal structure of the Yersinia type III secretion protein YscE. Protein Sci. 14 (2005) 2759-2763
28. Samatey F.A., Imada K., Nagashima S., Vonderviszt F., Kumasaka T., Yamamoto M., and Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410 (2001) 331-337
29. Picking W.L., Mertz J.A., Marquart M.E., and Picking W.D. Cloning, expression, and affinity purification of recombinant Shigella flexneri invasion plasmid antigens IpaB and IpaC. Protein Expr. Purif. 8 (1996) 401-408
30. 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115 (1993) 12593-12594
31. Tolman J.R., Chung J., and Prestegard J.H. Pure-phase heteronuclear multiple-quantum spectroscopy using field gradient selection. J. Magn. Reson. 98 (1992) 462-467
32. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
33. Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278 (2004) 313-352
34. Guntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278 (2004) 353-378
35. Dames S.A., Martinez-Yamout M., De Guzman R.N., Dyson H.J., and Wright P.E. Structural basis for Hif-1 alpha/CBP recognition in the cellular hypoxic response. Proc. Natl Acad. Sci. USA 99 (2002) 5271-5276
36. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
37. Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55