Structure of a kinesin-tubulin complex and implications for kinesin motility.

Abstract:

:The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.

journal_name

Nat Struct Mol Biol

authors

Gigant B,Wang W,Dreier B,Jiang Q,Pecqueur L,Plückthun A,Wang C,Knossow M

doi

10.1038/nsmb.2624

subject

Has Abstract

pub_date

2013-08-01 00:00:00

pages

1001-7

issue

8

eissn

1545-9993

issn

1545-9985

pii

nsmb.2624

journal_volume

20

pub_type

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