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Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin.

Abstract：

:Mg-ADP release is considered to be a crucial process for the regulation and motility of kinesin. To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release. On the basis of new structural and mutagenesis data, we propose a model mechanism for microtubule activation of Mg-ADP release from KIF1A. In our model, a specific interaction between loop L7 of KIF1A and beta-tubulin reconfigures the KIF1A active site by shifting the relative positions of switches I and II. This leads to the sequential release of a group of water molecules that sits over the Mg(2+) in the active site, followed by Mg(2+) and finally the ADP. We further propose that this set of events is linked to a strain-dependent docking of the neck linker to the motor core, which produces a two-step power stroke.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Nitta R,Okada Y,Hirokawa N

doi

10.1038/nsmb.1487

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

1067-75

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb.1487

journal_volume

15

pub_type

杂志文章

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