1zwt: Difference between revisions

Revision as of 18:49, 28 July 2008

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File:1zwt.png

Template:STRUCTURE 1zwt

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

Template:ABSTRACT PUBMED 16172128

About this StructureAbout this Structure

1ZWT is a Single protein structure of sequence from Escherichia coli. Full experimental 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

Complete resonance assignments of bundlin (BfpA) from the bundle-forming pilus of enteropathogenic Escherichia coli., Ramboarina S, Fernandes P, Simpson P, Frankel G, Donnenberg M, Matthews S, J Biomol NMR. 2004 Jul;29(3):427-8. PMID:15213452

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 {{STRUCTURE_1zwt|  PDB=1zwt  |  SCENE=  }}
-'''Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli'''
+===Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16172128}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16172128 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16172128}}
 ==About this Structure==
-ZWT is a [[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].
+ZWT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWT OCA].
 ==Reference==
 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:[http://www.ncbi.nlm.nih.gov/pubmed/16172128 16172128]
+Complete resonance assignments of bundlin (BfpA) from the bundle-forming pilus of enteropathogenic Escherichia coli., Ramboarina S, Fernandes P, Simpson P, Frankel G, Donnenberg M, Matthews S, J Biomol NMR. 2004 Jul;29(3):427-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15213452 15213452]
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
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 [[Category: Beta-sandwich]]
 [[Category: One disulfide bond]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:10:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:49:23 2008''