1zwt: Difference between revisions

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New page: left|200px<br /><applet load="1zwt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwt" /> '''Structure of the globular head domain of the...
 
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'''Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli'''<br />
'''Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli'''<br />


==Overview==
==Overview==
Bundle-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.
Bundle-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.


==About this Structure==
==About this Structure==
1ZWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZWT OCA].  
1ZWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWT OCA].  


==Reference==
==Reference==
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[[Category: Booy, F.]]
[[Category: Booy, F.]]
[[Category: Daniell, S.]]
[[Category: Daniell, S.]]
[[Category: Donnenberg, M.S.]]
[[Category: Donnenberg, M S.]]
[[Category: Fernandes, P.J.]]
[[Category: Fernandes, P J.]]
[[Category: Frankel, G.]]
[[Category: Frankel, G.]]
[[Category: Islam, S.]]
[[Category: Islam, S.]]
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[[Category: one disulfide bond]]
[[Category: one disulfide bond]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:53 2008''

Revision as of 17:19, 21 February 2008

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1zwt

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Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli

OverviewOverview

Bundle-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.

About this StructureAbout this Structure

1ZWT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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