The molecular mechanism of the type IVa pilus motors

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...

Full description

Bibliographic Details
Main Authors: Matthew McCallum, Stephanie Tammam, Ahmad Khan, Lori L. Burrows, P. Lynne Howell
Format: Article
Language:English
Published: Nature Publishing Group 2017-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms15091
id doaj-6b3b5867680949b9922cb7cf172605e1
record_format Article
spelling doaj-6b3b5867680949b9922cb7cf172605e12021-05-11T07:09:18ZengNature Publishing GroupNature Communications2041-17232017-05-018111010.1038/ncomms15091The molecular mechanism of the type IVa pilus motorsMatthew McCallum0Stephanie Tammam1Ahmad Khan2Lori L. Burrows3P. Lynne Howell4Department of Biochemistry, University of TorontoProgram in Molecular Medicine, 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 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.https://doi.org/10.1038/ncomms15091
collection DOAJ
language English
format Article
sources DOAJ
author Matthew McCallum
Stephanie Tammam
Ahmad Khan
Lori L. Burrows
P. Lynne Howell
spellingShingle Matthew McCallum
Stephanie Tammam
Ahmad Khan
Lori L. Burrows
P. Lynne Howell
The molecular mechanism of the type IVa pilus motors
Nature Communications
author_facet Matthew McCallum
Stephanie Tammam
Ahmad Khan
Lori L. Burrows
P. Lynne Howell
author_sort Matthew McCallum
title The molecular mechanism of the type IVa pilus motors
title_short The molecular mechanism of the type IVa pilus motors
title_full The molecular mechanism of the type IVa pilus motors
title_fullStr The molecular mechanism of the type IVa pilus motors
title_full_unstemmed The molecular mechanism of the type IVa pilus motors
title_sort molecular mechanism of the type iva pilus motors
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-05-01
description 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.
url https://doi.org/10.1038/ncomms15091
work_keys_str_mv AT matthewmccallum themolecularmechanismofthetypeivapilusmotors
AT stephanietammam themolecularmechanismofthetypeivapilusmotors
AT ahmadkhan themolecularmechanismofthetypeivapilusmotors
AT lorilburrows themolecularmechanismofthetypeivapilusmotors
AT plynnehowell themolecularmechanismofthetypeivapilusmotors
AT matthewmccallum molecularmechanismofthetypeivapilusmotors
AT stephanietammam molecularmechanismofthetypeivapilusmotors
AT ahmadkhan molecularmechanismofthetypeivapilusmotors
AT lorilburrows molecularmechanismofthetypeivapilusmotors
AT plynnehowell molecularmechanismofthetypeivapilusmotors
_version_ 1721452742118998016