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A metal switch for controlling the activity of molecular motor proteins.
- Source :
-
Nature Structural & Molecular Biology . Jan2012, Vol. 19 Issue 1, p122-127. 6p. 1 Diagram, 1 Chart, 4 Graphs. - Publication Year :
- 2012
-
Abstract
- Kinesins are molecular motors that require a divalent metal ion (for example, Mg2+) to convert the energy of ATP hydrolysis into directed force production along microtubules. Here we present the crystal structure of a recombinant kinesin motor domain bound to Mn2+ and ADP and report on a serine-to-cysteine substitution in the switch 1 motif of kinesin that allows its ATP hydrolysis activity to be controlled by adjusting the ratio of Mn2+ to Mg2+. This mutant kinesin binds ATP similarly in the presence of either metal ion, but its ATP hydrolysis activity is greatly diminished in the presence of Mg2+. In human kinesin-1 and kinesin-5 as well as Drosophila melanogaster kinesin-10 and kinesin-14, this defect is rescued by Mn2+, providing a way to control both the enzymatic activity and force-generating ability of these nanomachines. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15459993
- Volume :
- 19
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Nature Structural & Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 70121728
- Full Text :
- https://doi.org/10.1038/nsmb.2190