3PXN

Crystal structure of the Drosophila kinesin family member Kin10/NOD in complex with divalent manganese and ADP

Summary for 3PXN

• Entry DOI: 10.2210/pdb3pxn/pdb
• Related: 3dc4 3dcb 3dco
• Descriptor: Kinesin-like protein Nod, MANGANESE (II) ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: kinesin, motor domain, atp hydrolysis, meiosis, spindle protein, atp-binding, cell cycle, cell division, microtubule, motor protein, nucleotide-binding, alpha/beta class
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm, cytoskeleton (Probable): P18105
• Total number of polymer chains: 1
• Total formula weight: 38974.00

Authors

Cochran, J.C.,Zhao, Y.C.,Wilcox, D.E.,Kull, F.J. (deposition date: 2010-12-10, release date: 2011-12-21, Last modification date: 2023-09-13)

Primary citation

Cochran, J.C.,Zhao, Y.C.,Wilcox, D.E.,Kull, F.J.
A metal switch for controlling the activity of molecular motor proteins.
Nat.Struct.Mol.Biol., 19:122-127, 2012

PubMed Abstract: Kinesins are molecular motors that require a divalent metal ion (for example, Mg(2+)) 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 Mn(2+) 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 Mn(2+) to Mg(2+). 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 Mg(2+). In human kinesin-1 and kinesin-5 as well as Drosophila melanogaster kinesin-10 and kinesin-14, this defect is rescued by Mn(2+), providing a way to control both the enzymatic activity and force-generating ability of these nanomachines.

PubMed: 22198464
DOI: 10.1038/nsmb.2190

Experimental method

X-RAY DIFFRACTION (2.6 Å)