1rg0
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Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa
OverviewOverview
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 StructureAbout this Structure
1RG0 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
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
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