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Katanin spiral and ring structures shed light on power stroke for microtubule severing.

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Zehr E,Szyk A,Piszczek G,Szczesna E,Zuo X,Roll-Mecak A

doi

10.1038/nsmb.3448

subject

Has Abstract

pub_date

2017-09-01 00:00:00

pages

717-725

issue

9

eissn

1545-9993

issn

1545-9985

pii

nsmb.3448

journal_volume

24

pub_type

杂志文章

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