NDLI: Structure of the Type III Secretion Effector Protein ExoU in Complex with Its Chaperone SpcU

Content Provider	PubMed Central
Author	Halavaty, Andrei S. Borek, Dominika Tyson, Gregory H. Veesenmeyer, Jeff L. Shuvalova, Ludmilla George, Minasov Otwinowski, Zbyszek Hauser, Alan R. Anderson, Wayne F.
Editor	Kaufmann, Gunnar F.
Copyright Year	2012
Abstract	Disease causing bacteria often manipulate host cells in a way that facilitates the infectious process. Many pathogenic gram-negative bacteria accomplish this by using type III secretion systems. In these complex secretion pathways, bacterial chaperones direct effector proteins to a needle-like secretion apparatus, which then delivers the effector protein into the host cell cytosol. The effector protein ExoU and its chaperone SpcU are components of the Pseudomonas aeruginosa type III secretion system. Secretion of ExoU has been associated with more severe infections in both humans and animal models. Here we describe the 1.92 Å X-ray structure of the ExoU–SpcU complex, a full-length type III effector in complex with its full-length cognate chaperone. Our crystallographic data allow a better understanding of the mechanism by which ExoU kills host cells and provides a foundation for future studies aimed at designing inhibitors of this potent toxin.
Related Links	http://dx.doi.org/10.1371/journal.pone.0049388
Starting Page	49388
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	11
Volume Number	7
Language	English
Publisher	Public Library of Science
Publisher Date	2012-11-01
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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