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| Title | Katanin spiral and ring structures shed light on power stroke for microtubule severing. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Vol. 24, Issue 9, Page 717-725, Year 2017 |
| Publish date | Aug 7, 2017 |
 Authors | Elena Zehr / Agnieszka Szyk / Grzegorz Piszczek / Ewa Szczesna / Xiaobing Zuo / Antonina Roll-Mecak /  |
| 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 ...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. |
 External links | Nat Struct Mol Biol / PubMed:28783150 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 3.3 - 6.0 Å |
| Structure data | EMDB-8794, PDB-5wc0: EMDB-8796, PDB-5wcb:  PDB-5wc1: |
| Chemicals |  ChemComp-ATP:  ChemComp-SO4: |
| Source |
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 Keywords |  MOTOR PROTEIN / Microtubule cytoskeleton / microtubule-severing enzyme / AAA ATPase / p60 / CYTOSOLIC PROTEIN / microtubule severing enzyme / microtubule severing protein |
