Premium
Review: Structure and mechanism of the dynein motor ATPase
Author(s) -
Schmidt Helgo,
Carter Andrew P.
Publication year - 2016
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22856
Subject(s) - dynein , microtubule , atp hydrolysis , atpase , chemistry , motor protein , molecular motor , biophysics , aaa proteins , microbiology and biotechnology , mechanism (biology) , structural biology , gtp' , biochemistry , stereochemistry , enzyme , biology , physics , quantum mechanics
Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C‐terminal 3500 amino‐acid residues form the motor domain, which hydrolyses ATP in its ring of AAA+ (ATPases associated with diverse cellular activities) domains to generate the force for movement. The production of force is synchronized with cycles of microtubule binding and release, another important prerequisite for efficient motility along the microtubule. Although the large scale conformational changes that lead to force production and microtubule affinity regulation are well established, it has been largely enigmatic how ATP‐hydrolysis in the AAA+ ring causes these rearrangements. The past five years have seen a surge of high resolution information on the dynein motor domain that finally allowed unprecedented insights into this important open question. This review, part of the “ATP and GTP hydrolysis in Biology” special issue, will summarize our current understanding of the dynein motor mechanism with a special emphasis on the recently obtained crystal and EM structures. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 557–567, 2016.