5nd4 | pdb_00005nd4

Microtubule-bound MKLP2 motor domain in the presence of ADP.AlFx

spinqualitylabelsall models 5nd4, resolution 4.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nd4 is a 3 chain structure with sequence from [1] and Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ALF, GDP, GTP, MG, TA1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KI20A_MOUSE] Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle (By similarity). Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. [TBB2B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [F2Z4C1_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.[RuleBase:RU000352][SAAS:SAAS00824325] Publication Abstract from PubMed MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% identity) and size (~40% larger) compared to other kinesins. Using cryo-electron microscopy and biophysical assays, we have undertaken a mechanochemical dissection of the microtubule-bound MKLP2 motor domain during its ATPase cycle, and show that many facets of its mechanism are distinct from other kinesins. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. Furthermore, the footprint of the MKLP2 motor domain on the MT surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences. The conformation of the highly extended loop6 insertion characteristic of kinesin-6s is nucleotide-independent and does not contact the MT surface. Our results emphasize the role of family-specific insertions in modulating kinesin motor function. The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry.,Atherton J, Yu IM, Cook A, Muretta JM, Joseph A, Major J, Sourigues Y, Clause J, Topf M, Rosenfeld SS, Houdusse A, Moores CA Elife. 2017 Aug 11;6. pii: e27793. doi: 10.7554/eLife.27793. PMID:28826477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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