A Molecular Dynamics Study of Pilus Subunits: Insights into Pilus Biogenesis

Journal of Molecular Biology

Volumn 367, Issue 4, 2007, Pages 935-941

  Vitagliano, Luigi ^a   Ruggiero, Alessia ^a   Pedone, Carlo ^a,b   Berisio, Rita ^a  

^a CNR   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

bioinformatics; chaperone; donor strand exchange; protein protein interaction

Indexed keywords

CHAPERONE; ESCHERICHIA COLI PROTEIN; PILIN; PROTEIN PAPD; PROTEIN PAPE; PROTEIN PAPK; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM PILUS; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS);

EID: 33847716307     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.034     Document Type: Article

References (33)

1. Chen C.P., Posy S., Ben-Shaul A., Shapiro L., and Honig B.H. Specificity of cell-cell adhesion by classical cadherins: critical role for low-affinity dimerization through beta-strand swapping. Proc. Natl Acad. Sci. USA 102 (2005) 8531-8536
2. Guo Z., and Eisenberg D. Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proc. Natl Acad. Sci. USA 103 (2006) 8042-8047
3. Bennett M.J., Sawaya M.R., and Eisenberg D. Deposition diseases and 3D domain swapping. Structure 14 (2006) 811-824
4. Krasan G.P., Sauer F.G., Cutter D., Farley M.M., Gilsdorf J.R., Hultgren S.J., and St Geme III J.W. Evidence for donor strand complementation in the biogenesis of Haemophilus influenzae haemagglutinating pili. Mol. Microbiol. 35 (2000) 1335-1347
5. Remaut H., and Waksman G. Protein-protein interaction through beta-strand addition. Trends Biochem. Sci. 31 (2006) 436-444
6. Sauer F.G., Mulvey M.A., Schilling J.D., Martinez J.J., and Hultgren S.J. Bacterial pili: molecular mechanisms of pathogenesis. Curr. Opin. Microbiol. 3 (2000) 65-72
7. Ng T.W., Akman L., Osisami M., and Thanassi D.G. The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events. J. Bacteriol. 186 (2004) 5321-5331
8. Henderson N.S., So S.S., Martin C., Kulkarni R., and Thanassi D.G. Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling. J. Biol. Chem. 279 (2004) 53747-53754
9. Li H., Qian L., Chen Z., Thibault D., Liu G., Liu T., and Thanassi D.G. The outer membrane usher forms a twin-pore secretion complex. J. Mol. Biol. 344 (2004) 1397-1407
10. Dodson K.W., Jacob-Dubuisson F., Striker R.T., and Hultgren S.J. Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc. Natl Acad. Sci. USA 90 (1993) 3670-3674
11. Bullitt E., and Makowski L. Structural polymorphism of bacterial adhesion pili. Nature 373 (1995) 164-167
12. Sauer F.G., Futterer K., Pinkner J.S., Dodson K.W., Hultgren S.J., and Waksman G. Structural basis of chaperone function and pilus biogenesis. Science 285 (1999) 1058-1061
13. Sauer F.G., Pinkner J.S., Waksman G., and Hultgren S.J. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111 (2002) 543-551
14. Kuehn M.J., Ogg D.J., Kihlberg J., Slonim L.N., Flemmer K., Bergfors T., and Hultgren S.J. Structural basis of pilus subunit recognition by the PapD chaperone. Science 262 (1993) 1234-1241
15. Holmgren A., and Branden C.I. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342 (1989) 248-251
16. Nishiyama M., Horst R., Eidam O., Herrmann T., Ignatov O., and Vetsch M. et al Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. EMBO J. 24 (2005) 2075-2086
17. Nishiyama M., Vetsch M., Puorger C., Jelesarov I., and Glockshuber R. Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD. J. Mol. Biol. 330 (2003) 513-525
18. Choudhury D., Thompson A., Stojanoff V., Langermann S., Pinkner J., Hultgren S.J., and Knight S.D. X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science 285 (1999) 1061-1066
19. Hermanns U., Sebbel P., Eggli V., and Glockshuber R. Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli. Biochemistry 39 (2000) 11564-11570
20. Zavialov A.V., Berglund J., Pudney A.F., Fooks L.J., Ibrahim T.M., MacIntyre S., and Knight S.D. Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113 (2003) 587-596
21. Bann J.G., Pinkner J.S., Frieden C., and Hultgren S.J. Catalysis of protein folding by chaperones in pathogenic bacteria. Proc. Natl Acad. Sci. USA 101 (2004) 17389-17393
22. Vetsch M., Sebbel P., and Glockshuber R. Chaperone-independent folding of type 1 pilus domains. J. Mol. Biol. 322 (2002) 827-840
23. Aberg V., Hedenstrom M., Pinkner J.S., Hultgren S.J., and Almqvist F. C-Terminal properties are important for ring-fused 2-pyridones that interfere with the chaperone function in uropathogenic E. coli. Org. Biomol. Chem. 3 (2005) 3886-3892
24. Hedenstrom M., Emtenas H., Pemberton N., Aberg V., Hultgren S.J., Pinkner J.S., et al. NMR studies of interactions between periplasmic chaperones from uropathogenic E. coli and pilicides that interfere with chaperone function and pilus assembly. Org. Biomol. Chem. 3 (2005) 4193-4200
25. Pinkner J.S., Remaut H., Buelens F., Miller E., Aberg V., Pemberton N., et al. Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria. Proc. Natl Acad. Sci. USA 103 (2006) 17897-17902
26. Vetsch M., Erilov D., Moliere N., Nishiyama M., Ignatov O., and Glockshuber R. Mechanism of fibre assembly through the chaperone-usher pathway. EMBO Rep. 7 (2006) 734-738
27. Remaut H., Rose R.J., Hannan T.J., Hultgren S.J., Radford S.E., Ashcroft A.E., and Waksman G. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol. Cell 22 (2006) 831-842
28. Verger D., Miller E., Remaut H., Waksman G., and Hultgren S. Molecular mechanism of P pilus termination in uropathogenic Escherichia coli. EMBO Rep. 7 (2006) 1228-1232
29. Van Der Spoel D., Lindahl E., Hess B., Groenhof G., Mark A.E., and Berendsen H.J. GROMACS: fast, flexible, and free. J. Comput. Chem. 26 (2005) 1701-1718
30. Esposito L., Pedone C., and Vitagliano L. Molecular dynamics analyses of cross β-spine steric zipper models: β-sheet twisting and aggregation. Proc. Natl Acad. Sci. USA 103 (2006) 11533-11538
31. Merlino A., Esposito L., and Vitagliano L. Polyglutamine repeats and beta-helix structure: molecular dynamics study. Proteins: Struct. Funct. Genet. 63 (2006) 918-927
32. Kawata M., and Nagashima U. Particle mesh Ewald method for three-dimensional systems with two-dimensional periodicity. Chem. Phys. Letters 340 (2001) 165-172
33. Humphrey, W., Dalke, A. & Schulten, K. (1996) VMD: visual molecular dynamics. J. Mol. Graph. 14 33-38, 27-38.