7OD9
Crystal structure of activated CheY fused to the C-terminal domain of CheF
Summary for 7OD9
| Entry DOI | 10.2210/pdb7od9/pdb |
| Descriptor | Response regulator receiver protein, C-terminal domain of CheF from Methanococcus maripaludis, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | archaellum, chemotaxis, phosphorylation, motility, metal binding protein |
| Biological source | Methanococcus maripaludis X1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 56791.66 |
| Authors | Altegoer, F.,Weiland, P.,Bange, G. (deposition date: 2021-04-29, release date: 2022-04-27, Last modification date: 2024-01-31) |
| Primary citation | Altegoer, F.,Quax, T.E.F.,Weiland, P.,Nussbaum, P.,Giammarinaro, P.I.,Patro, M.,Li, Z.,Oesterhelt, D.,Grininger, M.,Albers, S.V.,Bange, G. Structural insights into the mechanism of archaellar rotational switching. Nat Commun, 13:2857-2857, 2022 Cited by PubMed Abstract: Signal transduction via phosphorylated CheY towards the flagellum and the archaellum involves a conserved mechanism of CheY phosphorylation and subsequent conformational changes within CheY. This mechanism is conserved among bacteria and archaea, despite substantial differences in the composition and architecture of archaellum and flagellum, respectively. Phosphorylated CheY has higher affinity towards the bacterial C-ring and its binding leads to conformational changes in the flagellar motor and subsequent rotational switching of the flagellum. In archaea, the adaptor protein CheF resides at the cytoplasmic face of the archaeal C-ring formed by the proteins ArlCDE and interacts with phosphorylated CheY. While the mechanism of CheY binding to the C-ring is well-studied in bacteria, the role of CheF in archaea remains enigmatic and mechanistic insights are absent. Here, we have determined the atomic structures of CheF alone and in complex with activated CheY by X-ray crystallography. CheF forms an elongated dimer with a twisted architecture. We show that CheY binds to the C-terminal tail domain of CheF leading to slight conformational changes within CheF. Our structural, biochemical and genetic analyses reveal the mechanistic basis for CheY binding to CheF and allow us to propose a model for rotational switching of the archaellum. PubMed: 35606361DOI: 10.1038/s41467-022-30358-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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