1zwt: Difference between revisions

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[[Image:1zwt.gif|left|200px]]<br /><applet load="1zwt" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zwt.gif|left|200px]]<br /><applet load="1zwt" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zwt" />

'''Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli'''<br />

==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==

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==

Line 15:

[[Category: Booy, F.]]

[[Category: Daniell, S.]]

[[Category: Donnenberg, M.S.]]

[[Category: Donnenberg, M S.]]

[[Category: Fernandes, P.J.]]

[[Category: Fernandes, P J.]]

[[Category: Frankel, G.]]

[[Category: Islam, S.]]

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[[Category: one disulfide bond]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 07:42:~~35 2007~~''

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

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@@ Line 1: / Line 1: @@
-[[Image:1zwt.gif|left|200px]]<br /><applet load="1zwt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zwt.gif|left|200px]]<br /><applet load="1zwt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zwt" />
 '''Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli'''<br />
 ==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==
-ZWT 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].
+ZWT 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==
@@ Line 15: / Line 15: @@
 [[Category: Booy, F.]]
 [[Category: Daniell, S.]]
-[[Category: Donnenberg, M.S.]]
+[[Category: Donnenberg, M S.]]
-[[Category: Fernandes, P.J.]]
+[[Category: Fernandes, P J.]]
 [[Category: Frankel, G.]]
 [[Category: Islam, S.]]
@@ Line 25: / Line 25: @@
 [[Category: one disulfide bond]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:42:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:53 2008''