1dzo

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Revision as of 14:34, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1dzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dzo, resolution 1.63Å" /> '''TRUNCATED PAK PILIN ...)
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File:1dzo.jpg


1dzo, resolution 1.63Å

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TRUNCATED PAK PILIN FROM PSEUDOMONAS AERUGINOSA

OverviewOverview

Fibers of pilin monomers (pili) form the dominant adhesin of Pseudomonas, aeruginosa, and they play an important role in infections by this, opportunistic bacterial pathogen. Blocking adhesion is therefore a target, for vaccine development. The receptor-binding site is located in a, C-terminal disulphide-bonded loop of each pilin monomer, but functional, binding sites are displayed only at the tip of the pilus. A factor, complicating vaccination is that different bacterial strains produce, distinct, and sometimes highly divergent, pilin variants. It is surprising, that all strains still appear to bind a common receptor, asialo-GM1. Here, we present the 1.63 A crystal structure of pilin from P. aeruginosa strain, PAK. The structure shows that the proposed receptor-binding site is formed, by two beta-turns that create a surface dominated by main-chain atoms., Receptor specificity could therefore be maintained, whilst allowing, side-chain variation, if the main-chain conformation is conserved. The, location of the binding site relative to the proposed packing of the pilus, fiber raises new issues and suggests that the current fiber model may have, to be reconsidered. Finally, the structure of the C-terminal, disulphide-bonded loop will provide the template for the structure-based, design of a consensus sequence vaccine.

About this StructureAbout this Structure

1DZO is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding., Hazes B, Sastry PA, Hayakawa K, Read RJ, Irvin RT, J Mol Biol. 2000 Jun 16;299(4):1005-17. PMID:10843854

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