1dzo: Difference between revisions

Revision as of 13:22, 21 February 2008

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

Page seeded by OCA on Thu Feb 21 12:22:14 2008

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OCA

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-[[Image:1dzo.jpg|left|200px]]<br /><applet load="1dzo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dzo.jpg|left|200px]]<br /><applet load="1dzo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dzo, resolution 1.63&Aring;" />
 '''TRUNCATED PAK PILIN FROM PSEUDOMONAS AERUGINOSA'''<br />
 ==Overview==
-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.
+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 Structure==
-DZO 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=1DZO OCA].
+DZO 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=1DZO OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Hazes, B.]]
-[[Category: Read, R.J.]]
+[[Category: Read, R J.]]
 [[Category: adhesin]]
 [[Category: lectin]]
 [[Category: type iv pilin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:41:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:14 2008''