1RG0

Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa

Summary for 1RG0

• Entry DOI: 10.2210/pdb1rg0/pdb
• Related: 1AYZ 1DZO 1HPW 1OQV 1OQW 1QVE
• 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: 2003-11-10, release date: 2004-09-07, Last modification date: 2023-12-06)

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

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: 15350129
DOI: 10.1021/bi048957s

Experimental method

X-RAY DIFFRACTION (1.8 Å)