1OQW

Full-Length PAK Pilin from Pseudomonas aeruginosa

Summary for 1OQW

• Entry DOI: 10.2210/pdb1oqw/pdb
• Related: 1DZO 1OQV 1OR9 2PIL
• Descriptor: Fimbrial protein (2 entities in total)
• Functional Keywords: type iv pilin, fiber-forming protein, adhesion, pseudomonas aerugionosa, pak pilin, cell adhesion
• Biological source: Pseudomonas aeruginosa
• Cellular location: Fimbrium: P02973
• Total number of polymer chains: 2
• Total formula weight: 30042.36

Authors

Craig, L.,Arvai, A.S.,Forest, K.T.,Tainer, J.A. (deposition date: 2003-03-11, release date: 2003-06-03, Last modification date: 2024-10-30)

Primary citation

Craig, L.,Taylor, R.K.,Pique, M.E.,Adair, B.A.,Arvai, A.S.,Singh, M.,Lloyd, S.J.,Shin, D.S.,Getzoff, E.D.,Yeager, M.,Forest, K.T.,Tainer, J.A.
Type IV Pilin Structure and Assembly: X-Ray and EM Analyses of Vibrio cholerae Toxin-Coregulated Pilus and Pseudomonas aeruginosa PAK Pilin
Mol.Cell, 11:1139-1150, 2003

PubMed Abstract: Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.

PubMed: 12769840
DOI: 10.1016/S1097-2765(03)00170-9

Experimental method

X-RAY DIFFRACTION (2 Å)