Keywords: Adhesive Proteins, Chaperone, Donor-Strand Exchange, Molecular Dynamics, Protein-Protein Interactions, Bacterial Protein, Protein Papa, Unclassified Drug, Atpa Protein, E Coli, Escherichia Coli Protein, Fimbria Protein, Bacterium Pilus, Binding Site, Complex Formation, Conference Paper, Controlled Study, Molecular Model, Nonhuman, Priority Journal, Protein Domain, Protein Protein Interaction, Uropathogenic Escherichia Coli, Article, Chemistry, Computer Simulation, Protein Secondary Structure, Protein Tertiary Structure, Thermodynamics, Bacteria (microorganisms), Fimbriae Proteins, Protein Structure,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Università degli Studi di Napoli Federico II, via Mezzocannone 16, I-80134 Napoli, Italy
Dipartimento delle Scienze Biologiche, Sezione di Biostrutture, Università degli Studi di Napoli Federico II, via Mezzocannone 16, I-80134 Napoli, Italy
References: Hooton, T.M., Stamm, W.E., Diagnosis and treatment of uncomplicated urinary tract infection (1997) Infect. Dis. Clin. North Am, 11, pp. 551-58
Holmgren, A., Branden, C.I., Crystal structure of chaperone protein papd reveals an immunoglobulin fold (1989) Nature, 342, pp. 248-251
Sauer, F.G., Pinkner, J.S., Waksman, G., Hultgren, S.J., Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation (2002) Cell, 111, pp. 543-551
Sauer, F.G., Futterer, K., Pinkner, J.S., Dodson, K.W., Hultgren, S.J., Waksman, G., Structural basis of chaperone function and pilus biogenesis (1999) Science, 285, pp. 1058-1061
Zavialov, A.V., Berglund, J., Pudney, A.F., Fooks, L.J., Ibrahim, T.M., MacIntyre, S., Knight, S.D., Structure and biogenesis of the capsular f1 antigen from yersinia pestis: Preserved folding energy drives fiber formation (2003) Cell, 113, pp. 587-596
Zavialov, A.V., Tischenko, V.M., Fooks, L.J., Brandsdal, B.O., Aqvist, J., Zav'yalov, V.P., Macintyre, S., Knight, S.D., Resolving the energy paradox of chaperone/ usher-mediated fibre assembly (2005) Biochem. J, 389, pp. 685-694
Choudhury, D., Thompson, A., Stojanoff, V., Langermann, S., Pinkner, J., Hultgren, S.J., Knight, S.D., X-ray structure of the fimc-fimh chaperone-adhesin complex from uropathogenic escherichia coli (1999) Science, 285, pp. 1061-1066
Remaut, H., Rose, R.J., Hannan, T.J., Hultgren, S.J., Radford, S.E., Ashcroft, A.E., Waksman, G., Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism (2006) Mol. Cells, 22, pp. 831-842
Verger, D., Bullitt, E., Hultgren, S.J., Waksman, G., Crystal structure of the p pilus rod subunit papa (2007) PLoS Pathog, 3, pp. e73
Remaut, H., Tang, C., Henderson, N.S., Pinkner, J.S., Wang, T., Hultgren, S.J., Thanassi, D.G., Li, H., Fiber formation across the bacterial outer membrane by the chaperone/usher pathway (2008) Cell, 133, pp. 640-652
Vitagliano, L., Ruggiero, A., Pedone, C., Berisio, R., A molecular dynamics study of pilus subunits: Insights into pilus biogenesis (2007) J. Mol. Biol, 367, pp. 935-941
Rose, R.J., Welsh, T.S., Waksman, G., Ashcroft, A.E., Radford, S.E., Paci, E., Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics (2008) J. Mol. Biol, 375, pp. 908-919
Jones, T.A., Interactive electron-density map interpretation: Frominter to o (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 2115-2125
Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A.E., Berendsen, H.J., Gromacs: Fast, flexible, and free (2005) J. Comput. Chem, 26, pp. 1701-1718
Scott, W.R.P., Huenenberger, P.H., Tironi, I.G., Mark, A.E., Billeter, S.R., Fennen, J., Torda, A.E., van Gunsteren, W.F., The gromos biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Jorgensen, W.L., Tirado-Rives, T., The opls forcefield for proteins. Energy minimizations for crystals of cyclic peptides and crambin (1988) J. Am. Chem. Soc, 110, pp. 1657-1666
Humphrey, W., Dalke, A., Schulten, K., Vmd: Visual molecular dynamics (1996) J. Mol. Graphics, 14, pp. 27-38. , 33-38
Mu Y, Kosov DS, Stock. G. Conformational dynamics of trialanine in water. 2. Comparison of amber, charmm, gromos, and opls force fields to nmr and infrared experiments. J. Phys. Chem. B 2003
107: 5064-5073Vetsch, M., Erilov, D., Moliere, N., Nishiyama, M., Ignatov, O., Glockshuber, R., Mechanism of fibre assembly through the chaperone-usher pathway (2006) EMBO Rep, 7, pp. 734-738
Verger, D., Miller, E., Remaut, H., Waksman, G., Hultgren, S., Molecular mechanism of p pilus termination in uropathogenic escherichia coli (2006) EMBO Rep, 7, pp. 1228-1232
Hooton, T. M., Stamm, W. E., Diagnosis and treatment of uncomplicated urinary tract infection (1997) Infect. Dis. Clin. North Am, 11, pp. 551-58
Sauer, F. G., Knight, S. D., Waksman, G. J., Hultgren, S. J., Papd-like chaperones and pilus biogenesis (2000) Semin. Cell Dev. Biol, 11, pp. 27-34
Sauer, F. G., Remaut, H., Hultgren, S. J., Waksman, G., Fiber assembly by the chaperone-usher pathway (2004) Biochim. Biophys. Acta, 1694, pp. 259-267
Zavialov, A. V., Kersley, J., Korpela, T., Zav'yalov, V. P., MacIntyre, S., Knight, S. D., Donor strand complementation mechanism in the biogenesis of non-pilus systems (2002) Mol. Microbiol, 45, pp. 983-995
Soto, G. E., Hultgren, S. J., Bacterial adhesins: Common themes and variations in architecture and assembly (1999) J. Bacteriol, 181, pp. 1059-1071
Dodson, K. W., Jacob-Dubuisson, F., Striker, R. T., Hultgren, S. J., Outermembrane papc molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes (1993) Proc. Natl. Acad. Sci. U. S. A, 90, pp. 3670-3674
Knight, S. D., Structure and assembly of yersinia pestis f1 antigen (2007) Adv. Exp. Med. Biol, 603, pp. 74-87
Sauer, F. G., Mulvey, M. A., Schilling, J. D., Martinez, J. J., Hultgren, S. J., Bacterial pili: Molecular mechanisms of pathogenesis (2000) Curr. Opin. Microbiol, 3, pp. 65-72
Sauer, F. G., Pinkner, J. S., Waksman, G., Hultgren, S. J., Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation (2002) Cell, 111, pp. 543-551
Sauer, F. G., Futterer, K., Pinkner, J. S., Dodson, K. W., Hultgren, S. J., Waksman, G., Structural basis of chaperone function and pilus biogenesis (1999) Science, 285, pp. 1058-1061
Zavialov, A. V., Berglund, J., Pudney, A. F., Fooks, L. J., Ibrahim, T. M., MacIntyre, S., Knight, S. D., Structure and biogenesis of the capsular f1 antigen from yersinia pestis: Preserved folding energy drives fiber formation (2003) Cell, 113, pp. 587-596
Zavialov, A. V., Tischenko, V. M., Fooks, L. J., Brandsdal, B. O., Aqvist, J., Zav'yalov, V. P., Macintyre, S., Knight, S. D., Resolving the energy paradox of chaperone/ usher-mediated fibre assembly (2005) Biochem. J, 389, pp. 685-694
Rose, R. J., Welsh, T. S., Waksman, G., Ashcroft, A. E., Radford, S. E., Paci, E., Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics (2008) J. Mol. Biol, 375, pp. 908-919
Jones, T. A., Interactive electron-density map interpretation: Frominter to o (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 2115-2125
Scott, W. R. P., Huenenberger, P. H., Tironi, I. G., Mark, A. E., Billeter, S. R., Fennen, J., Torda, A. E., van Gunsteren, W. F., The gromos biomolecular simulation program package (1999) J. Phys. Chem. A, 103, pp. 3596-3607
Jorgensen, W. L., Tirado-Rives, T., The opls forcefield for proteins. Energy minimizations for crystals of cyclic peptides and crambin (1988) J. Am. Chem. Soc, 110, pp. 1657-1666
Molecular dynamics studies of the P pilus rod subunit PapA