6a20 | pdb_00006a20

Crystal Structure of auto-inhibited Kinesin-3 KIF13B

spinqualitylabelsall models 6a20, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a20 is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, P6G Gene: Kif13b (Buffalo rat) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In kinesin-3, the coiled-coil 1 (CC1) can sequester the preceding neck coil (NC) for autoinhibition, but the underlying mechanism is poorly understood. Here, we determined the structures of the uninhibited motor domain (MD)-NC dimer and inhibited MD-NC-CC1 monomer of kinesin-3 KIF13B. In the MD-NC-CC1 monomer, CC1 is broken into two short helices that unexpectedly interact with both the NC and the MD. Compared with the MD-NC dimer, the CC1-mediated integration of NC and MD not only blocks the NC dimer formation, but also prevents the neck linker (NL) undocking and the ADP release from the MD. Mutations of the essential residues in the interdomain interaction interface in the MD-NC-CC1 monomer restored the MD activity. Thus, CC1 fastens the neck domain and MD and inhibits both NC and NL. This CC1-mediated lockdown of the entire neck domain may represent a paradigm for kinesin autoinhibition that could be applicable to other kinesin-3 motors. Coiled-coil 1-mediated fastening of the neck and motor domains for kinesin-3 autoinhibition.,Ren J, Wang S, Chen H, Wang W, Huo L, Feng W Proc Natl Acad Sci U S A. 2018 Dec 18;115(51):E11933-E11942. doi:, 10.1073/pnas.1811209115. Epub 2018 Nov 21. PMID:30463954 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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