5WC1
katanin AAA ATPase domain
Summary for 5WC1
| Entry DOI | 10.2210/pdb5wc1/pdb |
| Descriptor | Meiotic spindle formation protein mei-1, SULFATE ION (2 entities in total) |
| Functional Keywords | microtubule severing enzyme, cytosolic protein |
| Biological source | Caenorhabditis elegans |
| Cellular location | Cytoplasm, cytoskeleton, spindle pole : P34808 |
| Total number of polymer chains | 1 |
| Total formula weight | 51994.48 |
| Authors | Szyk, A.,Roll-Mecak, A. (deposition date: 2017-06-29, release date: 2017-08-09, Last modification date: 2023-10-04) |
| Primary citation | Zehr, E.,Szyk, A.,Piszczek, G.,Szczesna, E.,Zuo, X.,Roll-Mecak, A. Katanin spiral and ring structures shed light on power stroke for microtubule severing. Nat. Struct. Mol. Biol., 24:717-725, 2017 Cited by PubMed Abstract: Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing. PubMed: 28783150DOI: 10.1038/nsmb.3448 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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