Multiple conformations facilitate PilT function in the type IV pilus

Multiple conformations facilitate PilT function in the type IV pilus

Bacterial type IV pilus-like systems catalyse the formation of pilin fibres but it is unknown how they are powered. Here, the authors present crystal and cryo-EM structures of the hexameric motor ATPases PilB and PilT from Type IVa Pilus that reveal different conformational states, classify the conf...

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Main Authors: Matthew McCallum, Samir Benlekbir, Sheryl Nguyen, Stephanie Tammam, John L. Rubinstein, Lori L. Burrows, P. Lynne Howell
Format: Article
Language:English
Published: Nature Publishing Group 2019-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-13070-z
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spelling doaj-1255c099b54940abac6f1fa7758b58562021-05-11T12:13:48ZengNature Publishing GroupNature Communications2041-17232019-11-0110111610.1038/s41467-019-13070-zMultiple conformations facilitate PilT function in the type IV pilusMatthew McCallum0Samir Benlekbir1Sheryl Nguyen2Stephanie Tammam3John L. Rubinstein4Lori L. Burrows5P. Lynne Howell6Department of Biochemistry, University of TorontoProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick ChildrenProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick ChildrenProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick ChildrenDepartment of Biochemistry, University of TorontoDepartment of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Disease Research, McMaster UniversityDepartment of Biochemistry, University of TorontoBacterial type IV pilus-like systems catalyse the formation of pilin fibres but it is unknown how they are powered. Here, the authors present crystal and cryo-EM structures of the hexameric motor ATPases PilB and PilT from Type IVa Pilus that reveal different conformational states, classify the conformations of all PilT-like ATPase structures and propose a model for PilT function.https://doi.org/10.1038/s41467-019-13070-z
collection DOAJ
language English
format Article
sources DOAJ
author Matthew McCallum
Samir Benlekbir
Sheryl Nguyen
Stephanie Tammam
John L. Rubinstein
Lori L. Burrows
P. Lynne Howell
spellingShingle Matthew McCallum
Samir Benlekbir
Sheryl Nguyen
Stephanie Tammam
John L. Rubinstein
Lori L. Burrows
P. Lynne Howell
Multiple conformations facilitate PilT function in the type IV pilus
Nature Communications
author_facet Matthew McCallum
Samir Benlekbir
Sheryl Nguyen
Stephanie Tammam
John L. Rubinstein
Lori L. Burrows
P. Lynne Howell
author_sort Matthew McCallum
title Multiple conformations facilitate PilT function in the type IV pilus
title_short Multiple conformations facilitate PilT function in the type IV pilus
title_full Multiple conformations facilitate PilT function in the type IV pilus
title_fullStr Multiple conformations facilitate PilT function in the type IV pilus
title_full_unstemmed Multiple conformations facilitate PilT function in the type IV pilus
title_sort multiple conformations facilitate pilt function in the type iv pilus
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-11-01
description Bacterial type IV pilus-like systems catalyse the formation of pilin fibres but it is unknown how they are powered. Here, the authors present crystal and cryo-EM structures of the hexameric motor ATPases PilB and PilT from Type IVa Pilus that reveal different conformational states, classify the conformations of all PilT-like ATPase structures and propose a model for PilT function.
url https://doi.org/10.1038/s41467-019-13070-z
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AT johnlrubinstein multipleconformationsfacilitatepiltfunctioninthetypeivpilus
AT lorilburrows multipleconformationsfacilitatepiltfunctioninthetypeivpilus
AT plynnehowell multipleconformationsfacilitatepiltfunctioninthetypeivpilus
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