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1rg0
From Proteopedia
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[[Image:1rg0.gif|left|200px]] | [[Image:1rg0.gif|left|200px]] | ||
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'''Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa''' | '''Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa''' | ||
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[[Category: Hazes, B.]] | [[Category: Hazes, B.]] | ||
[[Category: Irvin, R T.]] | [[Category: Irvin, R T.]] | ||
| - | [[Category: | + | [[Category: Adhesin]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Pseudomona]] |
| - | [[Category: | + | [[Category: Type iv pilin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:27:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:27, 3 May 2008
Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa
Overview
Adherence of pathogens to host cells is critical for the initiation of infection and is thus an attractive target for anti-infective therapeutics and vaccines. In the opportunistic human pathogen Pseudomonas aeruginosa, host-cell adherence is achieved predominantly by type IV pili. Analysis of several clinical strains of P. aeruginosa reveals poor sequence conservation between pilin genes, including the residues in the receptor-binding site. Interestingly, the receptor-binding sites appear to retain a conserved surface epitope because all Pseudomonas type IV pili recognize the same receptor on the host cell and cross-reactive antibodies specific for the receptor-binding site exist. Here, we present the crystallographic analysis of two crystal forms of truncated pilin from P. aeruginosa strain K122-4 (DeltaK122-4) at 1.54 and 1.8 A resolution, respectively. The DeltaK122-4 structure is compared to other crystallographically determined type IV pilin structures and an NMR structure of DeltaK122-4 pilin. A comparison with the structure of the highly divergent P. aeruginosa strain K (DeltaPAK) pilin indicates that the receptor-binding loop in both pilins forms a shallow depression with a surface that is formed by main-chain atoms. Conservation of this putative binding site is independent of the sequence as long as the main-chain conformation is conserved and could therefore explain the shared receptor specificity and antibody cross reactivity of highly divergent Pseudomonas type IV pilins.
About this Structure
1RG0 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture., Audette GF, Irvin RT, Hazes B, Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:15350129 Page seeded by OCA on Sat May 3 07:27:05 2008
