7DMA
Crystal structure of FliM middle domain (46-231) with R49P substitution from Vibro alginolyticus
Summary for 7DMA
| Entry DOI | 10.2210/pdb7dma/pdb |
| Related | 7DM9 |
| Descriptor | Flagellar motor switch protein FliM (3 entities in total) |
| Functional Keywords | flagellar motor protein, motor protein |
| Biological source | Vibrio alginolyticus More |
| Total number of polymer chains | 2 |
| Total formula weight | 22231.75 |
| Authors | Takekawa, N.,Homma, M.,Imada, K. (deposition date: 2020-12-03, release date: 2021-07-07, Last modification date: 2023-11-29) |
| Primary citation | Takekawa, N.,Nishikino, T.,Yamashita, T.,Hori, K.,Onoue, Y.,Ihara, K.,Kojima, S.,Homma, M.,Imada, K. A slight bending of an alpha-helix in FliM creates a counterclockwise-locked structure of the flagellar motor in Vibrio. J.Biochem., 170:531-538, 2021 Cited by PubMed Abstract: Many bacteria swim by rotating flagella. The chemotaxis system controls the direction of flagellar rotation. Vibrio alginolyticus, which has a single polar flagellum, swims smoothly by rotating the flagellar motor counterclockwise (CCW) in response to attractants. In response to repellents, the motor frequently switches its rotational direction between CCW and clockwise (CW). We isolated a mutant strain that swims with a CW-locked rotation of the flagellum, which pulls rather than pushes the cell. This CW phenotype arises from a R49P substitution in FliM, which is the component in the C-ring of the motor that binds the chemotaxis signalling protein, phosphorylated CheY. However, this phenotype is independent of CheY, indicating that the mutation produces a CW conformation of the C-ring in the absence of CheY. The crystal structure of FliM with the R49P substitution showed a conformational change in the N-terminal α-helix of the middle domain of FliM (FliMM). This helix should mediates FliM-FliM interaction. The structural models of wild type and mutant C-ring showed that the relatively small conformational change in FliMM induces a drastic rearrangement of the conformation of the FliMM domain that generates a CW conformation of the C-ring. PubMed: 34143212DOI: 10.1093/jb/mvab074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.44 Å) |
Structure validation
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