5WC0

katanin hexamer in spiral conformation

Summary for 5WC0

• Entry DOI: 10.2210/pdb5wc0/pdb
• Related: 5WC1 5WCB
• EMDB information: 8794 8796
• Descriptor: Meiotic spindle formation protein mei-1, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: microtubule cytoskeleton, microtubule-severing enzyme, aaa atpase, p60, motor protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 6
• Total formula weight: 313857.24

Authors

Zehr, E.A.,Szyk, A.,Piszczek, G.,Szczesna, E.,Zuo, X.,Roll-Mecak, A. (deposition date: 2017-06-29, release date: 2017-08-09, Last modification date: 2024-03-13)

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

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: 28783150
DOI: 10.1038/nsmb.3448

Experimental method

ELECTRON MICROSCOPY (4.4 Å)