1p5u

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(New page: 200px<br /><applet load="1p5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5u, resolution 1.99&Aring;" /> '''X-ray structure of t...)
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[[Image:1p5u.jpg|left|200px]]<br /><applet load="1p5u" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1p5u.jpg|left|200px]]<br /><applet load="1p5u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p5u, resolution 1.99&Aring;" />
caption="1p5u, resolution 1.99&Aring;" />
'''X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex'''<br />
'''X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex'''<br />
==Overview==
==Overview==
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Most gram-negative pathogens express fibrous adhesive virulence organelles, that mediate targeting to the sites of infection. The F1 capsular antigen, from the plague pathogen Yersinia pestis consists of linear fibers of a, single subunit (Caf1) and serves as a prototype for nonpilus organelles, assembled via the chaperone/usher pathway. Genetic data together with, high-resolution X-ray structures corresponding to snapshots of the, assembly process reveal the structural basis of fiber formation., Comparison of chaperone bound Caf1 subunit with the subunit in the fiber, reveals a novel type of conformational change involving the entire, hydrophobic core of the protein. The observed conformational change, suggests that the chaperone traps a high-energy folding intermediate of, Caf1. A model is proposed in which release of the subunit allows folding, to be completed, driving fiber formation.
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Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.
==About this Structure==
==About this Structure==
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1P5U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P5U OCA].
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1P5U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5U OCA].
==Reference==
==Reference==
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[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
[[Category: Berglund, J.]]
[[Category: Berglund, J.]]
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[[Category: Fooks, L.J.]]
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[[Category: Fooks, L J.]]
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[[Category: Ibrahim, T.M.]]
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[[Category: Ibrahim, T M.]]
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[[Category: Knight, S.D.]]
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[[Category: Knight, S D.]]
[[Category: MacIntyre, S.]]
[[Category: MacIntyre, S.]]
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[[Category: Pudney, A.F.]]
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[[Category: Pudney, A F.]]
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[[Category: Zavialov, A.V.]]
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[[Category: Zavialov, A V.]]
[[Category: chaperone]]
[[Category: chaperone]]
[[Category: chaperone-subunit complex]]
[[Category: chaperone-subunit complex]]
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[[Category: protein fiber]]
[[Category: protein fiber]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:29:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:24 2008''

Revision as of 12:25, 21 February 2008


1p5u, resolution 1.99Å

Drag the structure with the mouse to rotate

X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex

Overview

Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.

About this Structure

1P5U is a Protein complex structure of sequences from Yersinia pestis. Full crystallographic information is available from OCA.

Reference

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation., Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD, Cell. 2003 May 30;113(5):587-96. PMID:12787500

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