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A major conformational change in p97 AAA ATPase upon ATP binding.

Abstract：

:AAA ATPases play central roles in cellular activities. The ATPase p97, a prototype of this superfamily, participates in organelle membrane fusion. Cryoelectron microscopy and single-particle analysis revealed that a major conformational change of p97 during the ATPase cycle occurred upon nucleotide binding and not during hydrolysis as previously hypothesized. Furthermore, our study indicates that six p47 adaptor molecules bind to the periphery of the ring-shaped p97 hexamer. Taken together, these results provide a revised model of how this and possibly other AAA ATPases can translate nucleotide binding into conformational changes of associated binding partners.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Rouiller I,Butel VM,Latterich M,Milligan RA,Wilson-Kubalek EM

doi

10.1016/s1097-2765(00)00144-1

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

1485-90

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)00144-1

journal_volume

6

pub_type

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