Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.
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ABSTRACT:
SUBMITTER: Paithankar KS
PROVIDER: S-EPMC6718144 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
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Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.
Paithankar Karthik Shivaji KS Enderle Mathias M Wirthensohn David C DC Miller Arthur A Schlesner Matthias M Pfeiffer Friedhelm F Rittner Alexander A Grininger Martin M Oesterhelt Dieter D
Acta crystallographica. Section F, Structural biology communications 20190830 Pt 9
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 ...[more]
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