1QVE
Crystal structure of the truncated K122-4 pilin from Pseudomonas aeruginosa
Summary for 1QVE
Entry DOI | 10.2210/pdb1qve/pdb |
Related | 1AYZ 1DZO 1HPW 1OQV 1OQW |
Descriptor | Fimbrial protein (2 entities in total) |
Functional Keywords | type iv pilin, lectin, adhesin, pseudomonas, cell adhesion |
Biological source | Pseudomonas aeruginosa |
Cellular location | Fimbrium: P17838 |
Total number of polymer chains | 2 |
Total formula weight | 25690.74 |
Authors | Audette, G.F.,Irvin, R.T.,Hazes, B. (deposition date: 2003-08-27, release date: 2004-09-07, Last modification date: 2024-11-06) |
Primary citation | Audette, G.F.,Irvin, R.T.,Hazes, B. Crystallographic Analysis of the Pseudomonas aeruginosa Strain K122-4 Monomeric Pilin Reveals a Conserved Receptor-Binding Architecture Biochemistry, 43:11427-11435, 2004 Cited by PubMed Abstract: 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. PubMed: 15350129DOI: 10.1021/bi048957s PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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