Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation

Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor...

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Autores principales: Paithankar, Karthik Shivaji, Enderle, Mathias, Wirthensohn, David C., Miller, Arthur, Schlesner, Matthias, Pfeiffer, Friedhelm, Rittner, Alexander, Grininger, Martin, Oesterhelt, Dieter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6718144/
https://www.ncbi.nlm.nih.gov/pubmed/31475924
http://dx.doi.org/10.1107/S2053230X19010896
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author Paithankar, Karthik Shivaji
Enderle, Mathias
Wirthensohn, David C.
Miller, Arthur
Schlesner, Matthias
Pfeiffer, Friedhelm
Rittner, Alexander
Grininger, Martin
Oesterhelt, Dieter
author_facet Paithankar, Karthik Shivaji
Enderle, Mathias
Wirthensohn, David C.
Miller, Arthur
Schlesner, Matthias
Pfeiffer, Friedhelm
Rittner, Alexander
Grininger, Martin
Oesterhelt, Dieter
author_sort Paithankar, Karthik Shivaji
collection PubMed
description Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor protein CheF. In this study, two new crystal forms and protein structures of CheY are reported. In both crystal forms, CheY is arranged in a domain-swapped conformation. CheF, the protein bridging the chemotaxis signal transduction system and the motility apparatus, was recombinantly expressed, purified and subjected to X-ray data collection.
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spelling pubmed-67181442019-09-09 Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation Paithankar, Karthik Shivaji Enderle, Mathias Wirthensohn, David C. Miller, Arthur Schlesner, Matthias Pfeiffer, Friedhelm Rittner, Alexander Grininger, Martin Oesterhelt, Dieter Acta Crystallogr F Struct Biol Commun Research Communications Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor protein CheF. In this study, two new crystal forms and protein structures of CheY are reported. In both crystal forms, CheY is arranged in a domain-swapped conformation. CheF, the protein bridging the chemotaxis signal transduction system and the motility apparatus, was recombinantly expressed, purified and subjected to X-ray data collection. International Union of Crystallography 2019-08-30 /pmc/articles/PMC6718144/ /pubmed/31475924 http://dx.doi.org/10.1107/S2053230X19010896 Text en © Paithankar et al. 2019 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Communications
Paithankar, Karthik Shivaji
Enderle, Mathias
Wirthensohn, David C.
Miller, Arthur
Schlesner, Matthias
Pfeiffer, Friedhelm
Rittner, Alexander
Grininger, Martin
Oesterhelt, Dieter
Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title_full Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title_fullStr Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title_full_unstemmed Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title_short Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation
title_sort structure of the archaeal chemotaxis protein chey in a domain-swapped dimeric conformation
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6718144/
https://www.ncbi.nlm.nih.gov/pubmed/31475924
http://dx.doi.org/10.1107/S2053230X19010896
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