Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin.

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Craig L,Taylor RK,Pique ME,Adair BD,Arvai AS,Singh M,Lloyd SJ,Shin DS,Getzoff ED,Yeager M,Forest KT,Tainer JA

doi

10.1016/s1097-2765(03)00170-9

subject

Has Abstract

pub_date

2003-05-01 00:00:00

pages

1139-50

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(03)00170-9

journal_volume

11

pub_type

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