3AJC
Structure of the MC domain of FliG (PEV), a CW-biased mutant
Summary for 3AJC
| Entry DOI | 10.2210/pdb3ajc/pdb |
| Descriptor | Flagellar motor switch protein fliG (2 entities in total) |
| Functional Keywords | chemotaxis, flagellum, flagellar motor, structural protein |
| Biological source | Thermotoga maritima |
| Cellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q9WY63 |
| Total number of polymer chains | 1 |
| Total formula weight | 26047.17 |
| Authors | Imada, K.,Minamino, T.,Kinoshita, M.,Namba, K. (deposition date: 2010-05-27, release date: 2011-05-11, Last modification date: 2024-03-13) |
| Primary citation | Minamino, T.,Imada, K.,Kinoshita, M.,Nakamura, S.,Morimoto, Y.V.,Namba, K. Structural insight into the rotational switching mechanism of the bacterial flagellar motor Plos Biol., 9:e1000616-e1000616, 2011 Cited by PubMed Abstract: The bacterial flagellar motor can rotate either clockwise (CW) or counterclockwise (CCW). Three flagellar proteins, FliG, FliM, and FliN, are required for rapid switching between the CW and CCW directions. Switching is achieved by a conformational change in FliG induced by the binding of a chemotaxis signaling protein, phospho-CheY, to FliM and FliN. FliG consists of three domains, FliG(N), FliG(M), and FliG(C), and forms a ring on the cytoplasmic face of the MS ring of the flagellar basal body. Crystal structures have been reported for the FliG(MC) domains of Thermotoga maritima, which consist of the FliG(M) and FliG(C) domains and a helix E that connects these two domains, and full-length FliG of Aquifex aeolicus. However, the basis for the switching mechanism is based only on previously obtained genetic data and is hence rather indirect. We characterized a CW-biased mutant (fliG(ΔPAA)) of Salmonella enterica by direct observation of rotation of a single motor at high temporal and spatial resolution. We also determined the crystal structure of the FliG(MC) domains of an equivalent deletion mutant variant of T. maritima (fliG(ΔPEV)). The FliG(ΔPAA) motor produced torque at wild-type levels under a wide range of external load conditions. The wild-type motors rotated exclusively in the CCW direction under our experimental conditions, whereas the mutant motors rotated only in the CW direction. This result suggests that wild-type FliG is more stable in the CCW state than in the CW state, whereas FliG(ΔPAA) is more stable in the CW state than in the CCW state. The structure of the TM-FliG(MC)(ΔPEV) revealed that extremely CW-biased rotation was caused by a conformational change in helix E. Although the arrangement of FliG(C) relative to FliG(M) in a single molecule was different among the three crystals, a conserved FliG(M)-FliG(C) unit was observed in all three of them. We suggest that the conserved FliG(M)-FliG(C) unit is the basic functional element in the rotor ring and that the PAA deletion induces a conformational change in a hinge-loop between FliG(M) and helix E to achieve the CW state of the FliG ring. We also propose a novel model for the arrangement of FliG subunits within the motor. The model is in agreement with the previous mutational and cross-linking experiments and explains the cooperative switching mechanism of the flagellar motor. PubMed: 21572987DOI: 10.1371/journal.pbio.1000616 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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