7X4N
Crystal Structure of C. elegans kinesin-4 KLP-12 complexed with tubulin and DARPin
Summary for 7X4N
Entry DOI | 10.2210/pdb7x4n/pdb |
Descriptor | Tubulin alpha-1A chain, Tubulin beta chain, DARPin, ... (8 entities in total) |
Functional Keywords | kinesin-4, klp-12, kif21a, kif21b, microtubule, tubulin, axon, cfeom1, darpin, motor protein |
Biological source | synthetic construct More |
Total number of polymer chains | 4 |
Total formula weight | 158355.42 |
Authors | Taguchi, S.,Imasaki, T.,Saijo-Hamano, Y.,Sakai, N.,Nitta, R. (deposition date: 2022-03-03, release date: 2022-09-21, Last modification date: 2023-11-29) |
Primary citation | Taguchi, S.,Nakano, J.,Imasaki, T.,Kita, T.,Saijo-Hamano, Y.,Sakai, N.,Shigematsu, H.,Okuma, H.,Shimizu, T.,Nitta, E.,Kikkawa, S.,Mizobuchi, S.,Niwa, S.,Nitta, R. Structural model of microtubule dynamics inhibition by kinesin-4 from the crystal structure of KLP-12 -tubulin complex. Elife, 11:-, 2022 Cited by PubMed Abstract: Kinesin superfamily proteins are microtubule-based molecular motors driven by the energy of ATP hydrolysis. Among them, the kinesin-4 family is a unique motor that inhibits microtubule dynamics. Although mutations of kinesin-4 cause several diseases, its molecular mechanism is unclear because of the difficulty of visualizing the high-resolution structure of kinesin-4 working at the microtubule plus-end. Here, we report that KLP-12, a kinesin-4 ortholog of KIF21A and KIF21B, is essential for proper length control of axons, and its motor domain represses microtubule polymerization in vitro. The crystal structure of the KLP-12 motor domain complexed with tubulin, which represents the high-resolution structural snapshot of the inhibition state of microtubule-end dynamics, revealed the bending effect of KLP-12 for tubulin. Comparison with the KIF5B-tubulin and KIF2C-tubulin complexes, which represent the elongation and shrinking forms of microtubule ends, respectively, showed the curvature of tubulin introduced by KLP-12 is in between them. Taken together, KLP-12 controls the proper length of axons by modulating the curvature of the microtubule ends to inhibit the microtubule dynamics. PubMed: 36065637DOI: 10.7554/eLife.77877 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.88 Å) |
Structure validation
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