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 1.99Å" /> '''X-ray structure of t...)
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Revision as of 21:22, 20 November 2007
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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
Page seeded by OCA on Tue Nov 20 23:29:53 2007
