1oqw

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(New page: 200px<br /><applet load="1oqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqw, resolution 2.0&Aring;" /> '''Full-Length PAK Pilin...)
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[[Image:1oqw.gif|left|200px]]<br /><applet load="1oqw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oqw, resolution 2.0&Aring;" />
caption="1oqw, resolution 2.0&Aring;" />
'''Full-Length PAK Pilin from Pseudomonas aeruginosa'''<br />
'''Full-Length PAK Pilin from Pseudomonas aeruginosa'''<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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1OQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQW OCA].
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1OQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQW OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arvai, A.S.]]
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[[Category: Arvai, A S.]]
[[Category: Craig, L.]]
[[Category: Craig, L.]]
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[[Category: Forest, K.T.]]
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[[Category: Forest, K T.]]
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[[Category: Tainer, J.A.]]
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[[Category: Tainer, J A.]]
[[Category: adhesion]]
[[Category: adhesion]]
[[Category: fiber-forming protein]]
[[Category: fiber-forming protein]]
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[[Category: type iv pilin]]
[[Category: type iv pilin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:06:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:42 2008''

Revision as of 12:20, 21 February 2008


1oqw, resolution 2.0Å

Drag the structure with the mouse to rotate

Full-Length PAK Pilin from Pseudomonas aeruginosa

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

1OQW is a Single protein structure of sequence from Pseudomonas aeruginosa. 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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