8yy5

Kinesin-14 with AlF3 bound to 14 PF Microtubule

spinqualitylabelsall models 8yy5, resolution 3.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8yy5 is a 4 chain structure with sequence from Drosophila melanogaster and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.99Å Ligands: ADP, ALF, GDP, GTP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TBA1B_PIG 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. Publication Abstract from PubMed Kinesin motor proteins hydrolyze ATP to produce force for spindle assembly and vesicle transport, performing essential functions in cell division and motility, but the structural changes required for force generation are uncertain. We now report high-resolution structures showing new transitions in the kinesin mechanochemical cycle, including power stroke fluctuations upon ATP binding and a post-hydrolysis state with bound ADP + free phosphate. We find that rate-limiting ADP release occurs upon microtubule binding, accompanied by central beta-sheet twisting, which triggers the power stroke - stalk rotation and neck mimic docking - upon ATP binding. Microtubule release occurs with beta-strand-to-loop transitions, implying that beta-strand refolding induces Pi release and the recovery stroke. The strained beta-sheet during the power stroke and strand-to-loop transitions identify the beta-sheet as the long-sought motor spring. Structural transitions in kinesin minus-end directed microtubule motility.,Shibata S, Wang MY, Imasaki T, Shigematsu H, Wei Y, Jobichen C, Hagio H, Sivaraman J, Endow SA, Nitta R bioRxiv [Preprint]. 2024 Jul 29:2024.07.29.605428. doi: , 10.1101/2024.07.29.605428. PMID:39131399 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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