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Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coliStructure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli
Structural highlights
FunctionBFPA_ECO27 Major repeating bundle-forming pilus (BFP) subunit. Is required for EPEC localized adherence. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBundle-forming pili (BFP) are essential for the full virulence of enteropathogenic Escherichia coli (EPEC) because they are required for localized adherence to epithelial cells and auto-aggregation. We report the high resolution structure of bundlin, the monomer of BFP, solved by NMR. The structure reveals a new variation in the topology of type IVb pilins with significant differences in the composition and relative orientation of elements of secondary structure. In addition, the structural parameters of native BFP filaments were determined by electron microscopy after negative staining. The solution structure of bundlin was assembled according to these helical parameters to provide a plausible atomic resolution model for the BFP filament. We show that EPEC and Vibriocholerae type IVb pili display distinct differences in their monomer subunits consistent with data showing that bundlin and TcpA cannot complement each other, but assemble into filaments with similar helical organization. Structure of the bundle-forming pilus from enteropathogenic Escherichia coli.,Ramboarina S, Fernandes PJ, Daniell S, Islam S, Simpson P, Frankel G, Booy F, Donnenberg MS, Matthews S J Biol Chem. 2005 Dec 2;280(48):40252-60. Epub 2005 Sep 19. PMID:16172128[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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