7wrg

Crystal structure of full-length kinesin-3 KLP-6

spinqualitylabelsall models 7wrg, resolution 3.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7wrg is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.16Å Ligands: ADP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G5EFQ4_CAEEL Publication Abstract from PubMed Autoinhibition of kinesin-3 ensures the proper spatiotemporal control of the motor activity for intracellular transport, but the underlying mechanism remains elusive. Here, we determine the full-length structure of kinesin-3 KLP-6 in a compact self-folded state. Unexpectedly, all the internal coiled-coil segments and domains in KLP-6 cooperate to successively lock down the neck and motor domains. The first coiled-coil segment is melted into several short helices that work with the motor domain to restrain the entire neck domain. The second coiled-coil segment associates with its neighboring FHA and MBS domains and integrates with the tail MATH domain to form a supramodule that synergistically wraps around the motor domain to trap the nucleotide and hinder the microtubule binding. This multilevel-lockdown mechanism for autoinhibition could be applicable to other kinesin-3 motors. The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition.,Wang W, Ren J, Song W, Zhang Y, Feng W Nat Commun. 2022 Jul 25;13(1):4281. doi: 10.1038/s41467-022-32048-y. PMID:35879313 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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