The molecular mechanism of the type IVa pilus motors

Matthew McCallum; Stephanie Tammam; Ahmad Khan; Lori L. Burrows; P. Lynne Howell

doi:10.1038/ncomms15091

Nature Communications (May 2017)

The molecular mechanism of the type IVa pilus motors

Matthew McCallum,
Stephanie Tammam,
Ahmad Khan,
Lori L. Burrows,
P. Lynne Howell

Affiliations

Matthew McCallum: Department of Biochemistry, University of Toronto
Stephanie Tammam: Program in Molecular Medicine, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children
Ahmad Khan: Department of Biochemistry, University of Toronto
Lori L. Burrows: Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Disease Research, McMaster University
P. Lynne Howell: Department of Biochemistry, University of Toronto

DOI: https://doi.org/10.1038/ncomms15091
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 10

Abstract

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Bacterial type IVa pili are protein filaments used for motility and protein secretion. Here the authors present crystal structures of theGeobacter metallireducensPilB ATPase in two nucleotide states, and suggest a clockwise rotation of the central sub-pores of PilB that would support the assembly of a right-handed helical pilus.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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