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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Autores principales:	Matthew McCallum, Samir Benlekbir, Sheryl Nguyen, Stephanie Tammam, John L. Rubinstein, Lori L. Burrows, P. Lynne Howell
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1255c099b54940abac6f1fa7758b5856
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spelling	oai:doaj.org-article:1255c099b54940abac6f1fa7758b58562021-12-02T15:35:58ZMultiple conformations facilitate PilT function in the type IV pilus10.1038/s41467-019-13070-z2041-1723https://doaj.org/article/1255c099b54940abac6f1fa7758b58562019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13070-zhttps://doaj.org/toc/2041-1723Bacterial 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.Matthew McCallumSamir BenlekbirSheryl NguyenStephanie TammamJohn L. RubinsteinLori L. BurrowsP. Lynne HowellNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
author	Matthew McCallum Samir Benlekbir Sheryl Nguyen Stephanie Tammam John L. Rubinstein Lori L. Burrows P. Lynne Howell
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 Portfolio
publishDate	2019
url	https://doaj.org/article/1255c099b54940abac6f1fa7758b5856
work_keys_str_mv	AT matthewmccallum multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT samirbenlekbir multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT sherylnguyen multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT stephanietammam multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT johnlrubinstein multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT lorilburrows multipleconformationsfacilitatepiltfunctioninthetypeivpilus AT plynnehowell multipleconformationsfacilitatepiltfunctioninthetypeivpilus
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Multiple conformations facilitate PilT function in the type IV pilus

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