Show simple item record

Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase

dc.contributor.authorSmith, Craig L.en_US
dc.contributor.authorKhandelwal, Purnimaen_US
dc.contributor.authorKeliikuli, Kaien_US
dc.contributor.authorZuiderweg, Erik R. P.en_US
dc.contributor.authorSaper, Mark A.en_US
dc.date.accessioned2010-06-01T19:18:47Z
dc.date.available2010-06-01T19:18:47Z
dc.date.issued2001-11en_US
dc.identifier.citationSmith, Craig L.; Khandelwal, Purnima; Keliikuli, Kai; Zuiderweg, Erik R. P.; Saper, Mark A. (2001). "Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase." Molecular Microbiology 42(4): 967-979. <http://hdl.handle.net/2027.42/72457>en_US
dc.identifier.issn0950-382Xen_US
dc.identifier.issn1365-2958en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/72457
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11737640&dopt=citationen_US
dc.format.extent2629652 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Science Ltden_US
dc.rightsBlackwell Science Ltden_US
dc.titleStructure of the type III secretion and substrate-binding domain of Yersinia YopH phosphataseen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI 48109-1055, USA.en_US
dc.contributor.affiliationotherDepartment of Biological Chemistry,en_US
dc.contributor.affiliationotherBiophysics Research Division anden_US
dc.identifier.pmid11737640en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/72457/1/j.0950-382x.2001.02711.x.pdf
dc.identifier.doi10.1046/j.0950-382x.2001.02711.xen_US
dc.identifier.sourceMolecular Microbiologyen_US
dc.identifier.citedreferenceAndersson, K., Carballeira, N., Magnusson, K.E., Persson, C., Stendahl, O., Wolf-Watz, H., Fallman, M. ( 1996 ) YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis. Mol Microbiol 20: 1057 – 1069en_US
dc.identifier.citedreferenceBailey, S. ( 1994 ) The CCP4 suite of programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760 – 763en_US
dc.identifier.citedreferenceBennett, M.J., Schlunegger, M.P., Eisenberg, D. ( 1995 ) 3D domain swapping: a mechanism for oligomer assembly. Protein Sci 4: 2455 – 2468en_US
dc.identifier.citedreferenceBirge, R.B., Fajardo, J.E., Reichman, C., Shoelson, S.E., Songyang, Z., Cantley, L.C., Hanafusa, H. ( 1993 ) Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol Cell Biol 13: 4648 – 4656en_US
dc.identifier.citedreferenceBlack, D.S. & Bliska, J.B. ( 1997 ) Identification of p130 Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J 16: 2730 – 2744en_US
dc.identifier.citedreferenceBlack, D.S., Montagna, L.G., Zitsmann, S., Bliska, J.B. ( 1998 ) Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets. Mol Microbiol 29: 1263 – 1274en_US
dc.identifier.citedreferenceBlack, D.S., Marie-Cardine, A., Schraven, B., Bliska, J.B. ( 2000 ) The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages. Cell Microbiol 2: 401 – 414en_US
dc.identifier.citedreferenceBliska, J.B. & Black, D.S. ( 1995 ) Inhibition of the Fc receptor-mediated oxidative burst in macrophages by the Yersinia pseudotuberculosis tyrosine phosphatase. Infect Immun 63: 681 – 685en_US
dc.identifier.citedreferenceBliska, J.B., Guan, K.L., Dixon, J.E., Falkow, S. ( 1991 ) Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc Natl Acad Sci USA 88: 1187 – 1191en_US
dc.identifier.citedreferenceBliska, J.B., Clemens, J.C., Dixon, J.E., Falkow, S. ( 1992 ) The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774A.1 macrophage. J Exp Med 176: 1625 – 1630en_US
dc.identifier.citedreferenceCambronne, E.D., Cheng, L.W., Schneewind, O. ( 2000 ) LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism. Mol Microbiol 37: 263 – 273en_US
dc.identifier.citedreferenceCarson, M. ( 1997 ) Ribbons. Methods Enzymol 277: 493 – 505en_US
dc.identifier.citedreferenceCavanagh, J., Fairbrother, W.J., Palmer, A.G., III, Skelton, N.J. ( 1996 ) Protein NMR Spectroscopy: Principles and Practice. San Diego: Academic Pressen_US
dc.identifier.citedreferenceCornelis, G.R. & Van Gijsegem, F. ( 2000 ) Assembly and function of type III secretory systems. Annu Rev Microbiol 54: 735 – 774en_US
dc.identifier.citedreferenceDaughdrill, G.W., Chadsey, M.S., Karlinsey, J.E., Hughes, K.T., Dahlquist, F.W. ( 1997 ) The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nature Struct Biol 4: 285 – 291en_US
dc.identifier.citedreferenceDaughdrill, G.W., Hanely, L.J., Dahlquist, F.W. ( 1998 ) The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations. Biochemistry 37: 1076 – 1082en_US
dc.identifier.citedreferenceDayie, K.T. & Wagner, G. ( 1994 ) Relaxation-rate measurements for 15 N- 1 H groups with pulsed-field gradients and preservation of coherence pathways. J Magn Reson A 111: 121 – 126en_US
dc.identifier.citedreferenceDelaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A. ( 1995 ) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277 – 293en_US
dc.identifier.citedreferenceDrenth, J. ( 1999 ) Principles of Protein X-Ray Crystallography. New York: Springeren_US
dc.identifier.citedreferenceEvdokimov, A.G., Tropea, J.E., Routzahn, K.M., Copeland, T.D., Waugh, D.S. ( 2001 ) Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 Å resolution. Acta Crystallogr D Biol Crystallogr 57: 793 – 799en_US
dc.identifier.citedreferenceFauman, E.B. & Saper, M.A. ( 1996 ) Structure and function of the protein tyrosine phosphatases. Trends Biochem Sci 21: 413 – 417en_US
dc.identifier.citedreferenceFinlay, B.B. & Cossart, P. ( 1997 ) Exploitation of mammalian host cell functions by bacterial pathogens. Science 276: 718 – 725en_US
dc.identifier.citedreferenceGuan, K.L. & Dixon, J.E. ( 1990 ) Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249: 553 – 556en_US
dc.identifier.citedreferenceHamid, N., Gustavsson, A., Andersson, K., McGee, K., Persson, C., Rudd, C.E., Fallman, M. ( 1999 ) YopH dephosphorylates Cas and Fyn-binding protein in macrophages. Microb Pathog 27: 231 – 242en_US
dc.identifier.citedreferenceHof, P., Pluskey, S., Dhe-Paganon, S., Eck, M.J., Shoelson, S.E. ( 1998 ) Crystal structure of the tyrosine phosphatase SHP-2. Cell 92: 441 – 450en_US
dc.identifier.citedreferenceHueck, C.J. ( 1998 ) Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62: 379 – 433en_US
dc.identifier.citedreferenceJohnson, B.A. & Blevins, R.A. ( 1994 ) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4: 603 – 614en_US
dc.identifier.citedreferenceJones, T.A., Zou, J.-Y., Cowan, S.W., Kjeldgaard, M. ( 1991 ) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110 – 119en_US
dc.identifier.citedreferenceKhandelwal, P., Keliikuli, K., Smith, C.L., Saper, M.A., Zuiderweg, E.R.P. ( 2001 ) 1 H, 15 N and 13 C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide. J Biomol NMR 21: 69 – 70en_US
dc.identifier.citedreferenceLiu, Y.S., Gotte, G., Libonati, M., Eisenberg, D. ( 2001 ) A domain-swapped RNase A dimer with implications for amyloid formation. Nature Struct Biol 8: 211 – 214en_US
dc.identifier.citedreferenceLloyd, S.A., 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 – 531en_US
dc.identifier.citedreferenceMacnab, R.M. ( 1999 ) The bacterial flagellum: reversible rotary propeller and type III export apparatus. J Bacteriol 181: 7149 – 7153en_US
dc.identifier.citedreferenceMcRee, D. ( 1996 ) Molecular Images Software [ http://www.concentric.net/~Molimage/ ]. San Diego: Molecular Images Software.en_US
dc.identifier.citedreferenceMontagna, L.G., Ivanov, M.I., Bliska, J.B. ( 2001 ) Identification of residues in the N-terminal domain of the Yersinia tyrosine phosphatase that are critical for substrate recognition. J Biol Chem 276: 5005 – 5011en_US
dc.identifier.citedreferenceNamba, K. ( 2001 ) Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells 6: 1 – 12en_US
dc.identifier.citedreferenceNewcomer, M.E. ( 2001 ) Trading places. Nature Struct Biol 8: 282 – 284en_US
dc.identifier.citedreferenceNicholls, A., Sharp, K.A., Honig, B. ( 1991 ) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281 – 296en_US
dc.identifier.citedreferenceOtwinowski, Z. & Minor, W. ( 1997 ) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307 – 326en_US
dc.identifier.citedreferencePeng, J.W. & Wagner, G. ( 1994 ) Protein mobility from multiple 15 N relaxation parameters. In Nuclear Magnetic Resonance Probes of Molecular Dynamics. Tycko, R. (eds). Dordrecht: Kluwer, pp. 373 – 454en_US
dc.identifier.citedreferencePersson, C., Carballeira, N., Wolf-Watz, H., Fallman, M. ( 1997 ) The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130 Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J 16: 2307 – 2318en_US
dc.identifier.citedreferenceRead, R.J. ( 1986 ) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42: 140 – 149en_US
dc.identifier.citedreferenceRimpilÄinen, M., Forsberg, Å., Wolf-Watz, H. ( 1992 ) A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH. J Bacteriol 174: 3355 – 3363en_US
dc.identifier.citedreferenceSakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., et al. ( 1994 ) A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 13: 3748 – 3756en_US
dc.identifier.citedreferenceSchiering, N., Casale, E., Caccia, P., Giordano, P., Battistini, C. ( 2000 ) Dimer formation through domain swapping in the crystal structure of the Grb2–SH2–Ac-pYVNV complex. Biochemistry 39: 13376 – 13382en_US
dc.identifier.citedreferenceSory, M.P., Boland, A., Lambermont, I., Cornelis, G.R. ( 1995 ) Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc Natl Acad Sci USA 92: 11998 – 12002en_US
dc.identifier.citedreferenceStainier, I., Iriarte, M., Cornelis, G.R. ( 1997 ) YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription. Mol Microbiol 26: 833 – 843en_US
dc.identifier.citedreferenceSu, X.D., Gastinel, L.N., Vaughn, D.E., Faye, I., Poon, P., Bjorkman, P.J. ( 1998 ) Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion. Science 281: 991 – 995en_US
dc.identifier.citedreferenceVijayalakshmi, J., Mukhergee, M.K., Graumann, J., Jakob, U., Saper, M.A. ( 2001 ) The 2.2  Å crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Structure 9: 367 – 375en_US
dc.identifier.citedreferenceWang, L.C., Pang, Y.X., Holder, T., Brender, J.R., Kurochkin, A.V., Zuiderweg, E.R.P. ( 2001 ) Functional dynamics in the active site of the ribonuclease binase. Proc Natl Acad Sci USA 98: 7684 – 7689en_US
dc.identifier.citedreferenceWoestyn, S., Sory, M.P., Boland, A., Lequenne, O., Cornelis, G.R. ( 1996 ) The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes. Mol Microbiol 20: 1261 – 1271en_US
dc.identifier.citedreferenceZhang, Z.-Y. & Dixon, J.E. ( 1994 ) Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity. Adv Enzymol Relat Areas Mol Biol 68: 1 – 36en_US
dc.identifier.citedreferenceZhang, Z.-Y., Clemens, J.C., Schubert, H.L., Stuckey, J.A., Fischer, M.W., Hume, D.M., et al. ( 1992 ) Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase. J Biol Chem 267: 23759 – 23766en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.