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Type IV Pilin Structures: Insights on Shared Architecture, Fiber Assembly, Receptor Binding and Type II Secretion

Hansen J.K. · Forest K.T.

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Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisc., USA

Related Articles for ""

J Mol Microbiol Biotechnol 2006;11:192–207

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Article / Publication Details

First-Page Preview
Abstract of Reviews

Published online: September 21, 2006
Issue release date: September 2006

Number of Print Pages: 16
Number of Figures: 4
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

Type IV pili are long, flexible filaments that extend from the surface of Gram-negative bacteria and are formed by the polymerization of pilin subunits. This review focuses on the structural information available for each pilin subclass, type IVa and type IVb, highlighting the contributions crystal and nuclear magnetic resonance structures have made in understanding pilus function and assembly. In addition, the type II secretion pseudopilus subunit structure and helical assembly is compared to that of the type IV pilus. The pilin subunits adopt an αβ-roll fold formed by the hydrophobic packing of the C-terminal half of a long α-helix against an antiparallel β-sheet. The conserved N-terminal half of the same α-helix, as well as two sequence- and structurally-variable regions, protrude from this globular head domain. Filament models have a hydrophobic core formed by the signature long α-helices, with variable regions at the filament surface.

© 2006 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Reviews

Published online: September 21, 2006
Issue release date: September 2006

Number of Print Pages: 16
Number of Figures: 4
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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