3dc4

Crystal structure of the Drosophila kinesin family member NOD in complex with ADP

spinqualitylabelsall models 3dc4, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dc4 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, MG Related: 3dcb Gene: nod, NODA, CG1763 (DROME) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Segregation of nonexchange chromosomes during Drosophila melanogaster meiosis requires the proper function of NOD, a nonmotile kinesin-10. We have determined the X-ray crystal structure of the NOD catalytic domain in the ADP- and AMPPNP-bound states. These structures reveal an alternate conformation of the microtubule binding region as well as a nucleotide-sensitive relay of hydrogen bonds at the active site. Additionally, a cryo-electron microscopy reconstruction of the nucleotide-free microtubule-NOD complex shows an atypical binding orientation. Thermodynamic studies show that NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including AMPPNP, are weakened. Our pre-steady-state kinetic analysis demonstrates that NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis, which is also atypical for a kinesin. We propose a model for NOD's microtubule plus-end tracking that drives chromosome movement. ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement.,Cochran JC, Sindelar CV, Mulko NK, Collins KA, Kong SE, Hawley RS, Kull FJ Cell. 2009 Jan 9;136(1):110-22. PMID:19135893 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin

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