3pxn | pdb_00003pxn

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

spinqualitylabelsall models 3pxn, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pxn is a 1 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MN Related: 3dc4, 3dcb, 3dco Gene: nod, NODA, CG1763 (DROME) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NOD_DROME] Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively "paired" chromosomes at the metaphase plate until anaphase. Publication Abstract from PubMed 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. A metal switch for controlling the activity of molecular motor proteins.,Cochran JC, Zhao YC, Wilcox DE, Kull FJ Nat Struct Mol Biol. 2011 Dec 25;19(1):122-7. doi: 10.1038/nsmb.2190. PMID:22198464 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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