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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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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2019-09, Vol.75 (9), p.576-585
Main Authors: Paithankar, Karthik Shivaji, Enderle, Mathias, Wirthensohn, David C., Miller, Arthur, Schlesner, Matthias, Pfeiffer, Friedhelm, Rittner, Alexander, Grininger, Martin, Oesterhelt, Dieter
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Language:English
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Summary: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. Che proteins are part of the signal transduction pathway between stimulus and response, mediated by the archaellum. The structure of the chemotaxis protein CheY was determined in two different crystal forms. The novel CheF protein that connects chemotaxis signaling to the motility apparatus was expressed and crystallized, and data were acquired by X‐ray diffraction.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X19010896