title: Crystal structure of the Yersinia type III secretion protein YscE.
abstract: The plague-causing bacterium Yersinia pestis utilizes a contact-dependent (type III) secretion system (T3SS) to transport virulence factors from the bacterial cytosol directly into the interior of mammalian cells where they interfere with signal transduction pathways that mediate phagocytosis and the inflammatory response. The type III secretion apparatus is composed of 20-25 different Yersinia secretion (Ysc) proteins. We report here the structure of YscE, the smallest Ysc protein, which is a dimer in solution. The probable mode of oligomerization is discussed.
authors.affiliation: Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA.
authors.forename: Jason
authors.initials: J
authors.lastname: Phan
authors.forename: Brian P
authors.initials: BP
authors.lastname: Austin
authors.forename: David S
authors.initials: DS
authors.lastname: Waugh
mesh_terms: D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D019281:Dimerization; D010587:Phagocytosis / Q000502:physiology; D021381:Protein Transport / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D037521:Virulence Factors / Q000378:metabolism; D015010:Yersinia pestis / Q000737:chemistry* / Q000502:physiology
chemical_list: D001425:Bacterial Outer Membrane Proteins; D037521:Virulence Factors