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Crystal structure of the Yersinia type III secretion protein YscE
Author(s) -
Phan Jason,
Austin Brian P.,
Waugh David S.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051706105
Subject(s) - yersinia pestis , secretion , cytosol , yersinia , virulence , type three secretion system , signal transduction , transport protein , phagocytosis , microbiology and biotechnology , chemistry , biology , bacteria , biochemistry , enzyme , gene , genetics
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.