1oqv

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(New page: 200px<br /><applet load="1oqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqv, resolution 1.3&Aring;" /> '''Structure of TcpA, th...)
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[[Image:1oqv.jpg|left|200px]]<br /><applet load="1oqv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oqv, resolution 1.3&Aring;" />
caption="1oqv, resolution 1.3&Aring;" />
'''Structure of TcpA, the Type IV pilin subunit from the toxin co-regulated pilus of Vibrio cholerae classical biotype'''<br />
'''Structure of TcpA, the Type IV pilin subunit from the toxin co-regulated pilus of Vibrio cholerae classical biotype'''<br />
==Overview==
==Overview==
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Pilin assembly into type IV pili is required for virulence by bacterial, pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and, meningitis. Crystal structures of soluble, N-terminally truncated pilin, from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK, pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared, architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the, structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the, extended hydrophobic alpha helices make multisubunit contacts to provide, mechanical strength and flexibility. Outside, distinct interactions of, adaptable heads contribute surface variation for specificity of pilus, function in antigenicity, motility, adhesion, and colony formation.
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Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.
==About this Structure==
==About this Structure==
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1OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].
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1OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].
==Reference==
==Reference==
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[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
[[Category: Craig, L.]]
[[Category: Craig, L.]]
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[[Category: Tainer, J.A.]]
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[[Category: Tainer, J A.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: adhesin]]
[[Category: adhesin]]
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[[Category: vibrio cholerae]]
[[Category: vibrio cholerae]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:06:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:43 2008''

Revision as of 12:20, 21 February 2008

Image:1oqv.jpg

1oqv, resolution 1.3Å

Drag the structure with the mouse to rotate

Structure of TcpA, the Type IV pilin subunit from the toxin co-regulated pilus of Vibrio cholerae classical biotype

Overview

Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.

About this Structure

1OQV is a Single protein structure of sequence from Vibrio cholerae with as ligand. Full crystallographic information is available from OCA.

Reference

Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin., Craig L, Taylor RK, Pique ME, Adair BD, Arvai AS, Singh M, Lloyd SJ, Shin DS, Getzoff ED, Yeager M, Forest KT, Tainer JA, Mol Cell. 2003 May;11(5):1139-50. PMID:12769840

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