Structural highlights
Publication Abstract from PubMed
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.
Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.,Paithankar KS, Enderle M, Wirthensohn DC, Miller A, Schlesner M, Pfeiffer F, Rittner A, Grininger M, Oesterhelt D Acta Crystallogr F Struct Biol Commun. 2019 Sep 1;75(Pt 9):576-585. doi:, 10.1107/S2053230X19010896. Epub 2019 Aug 30. PMID:31475924[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Paithankar KS, Enderle M, Wirthensohn DC, Miller A, Schlesner M, Pfeiffer F, Rittner A, Grininger M, Oesterhelt D. Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation. Acta Crystallogr F Struct Biol Commun. 2019 Sep 1;75(Pt 9):576-585. doi:, 10.1107/S2053230X19010896. Epub 2019 Aug 30. PMID:31475924 doi:http://dx.doi.org/10.1107/S2053230X19010896
