1DZO

Truncated PAK pilin from Pseudomonas aeruginosa

Summary for 1DZO

• Entry DOI: 10.2210/pdb1dzo/pdb
• Related: 1NIL 1NIM 1PAJ 1PAK
• Descriptor: TYPE IV PILIN (2 entities in total)
• Functional Keywords: lectin, adhesin, cell adhesion
• Biological source: PSEUDOMONAS AERUGINOSA PAK
• Total number of polymer chains: 1
• Total formula weight: 12696.23

Authors

Hazes, B.,Read, R.J. (deposition date: 2000-03-06, release date: 2000-06-11, Last modification date: 2024-11-20)

Primary citation

Hazes, B.,Sastry, P.A.,Hayakawa, K.,Read, R.J.,Irvin, R.T.
Crystal Structure of Pseudomonas Aeruginosa Pak Pilin Suggests a Main-Chain-Dominated Mode of Receptor Binding
J.Mol.Biol., 299:1005-, 2000

PubMed Abstract: 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.

PubMed: 10843854
DOI: 10.1006/JMBI.2000.3801

Experimental method

X-RAY DIFFRACTION (1.63 Å)