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- Title
Structure and biochemical analysis of a secretin pilot protein.
- Authors
Lario, Paula I.; Pfuetzner, Richard A.; Frey, Elizabeth A.; Creagh, Louise; Haynes, Charles; Maurelli, Anthony T.; Strynadka, Natalie C. J.
- Abstract
The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion apparatus, the assembly of the TTSS complex requires the preceding formation of its integral outer membrane secretin ring component. We have determined at 1.5Åthe structure of MxiM28-142, the Shigella pilot protein that is essential for the assembly and membrane association of the Shigella secretin, MxiD. This represents the first atomic structure of a secretin pilot protein from the several bacterial secretion systems containing an orthologous secretin component. A deep hydrophobic cavity is observed in the novel‘cracked barrel’structure of MxiM, providing a specific binding domain for the acyl chains of bacterial lipids, a proposal that is supported by our various lipid/MxiM complex structures. Isothermal titration analysis shows that the C-terminal domain of the secretin, MxiD525-570, hinders lipid binding to MxiM.
- Subjects
MICROBIAL virulence -- Molecular aspects; BACTERIAL proteins; CELLS; GRAM-negative bacteria; ESCHERICHIA coli; SECRETIN
- Publication
EMBO Journal, 2005, Vol 24, Issue 6, p1111
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1038/sj.emboj.7600610