ArticleActa crystallographica. Section F, Structural biology communications2019
Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023Article
- Structures of permuted halves of a modern ribose-binding protein.Acta crystallographica. Section D, Structural biology · 2023Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- Evolution, folding, and design of TIM barrels and related proteins.Current opinion in structural biology · 2021Review
- 3D Domain Swapping Dimerization of the Receiver Domain of Cytokinin Receptor CRE1 FromFrontiers in plant science · 2021Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.Chembiochem : a European journal of chemical biology · 2020Article
- The switch complex ArlCDE connects the chemotaxis system and the archaellum.Molecular microbiology · 2020Article
- Taking biological structure communications into the third dimension.Acta crystallographica. Section F, Structural biology communications · 2019Article
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Authors and funding
9 authors.
Funding
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Abstract
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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