7WRG
Crystal structure of full-length kinesin-3 KLP-6
Summary for 7WRG
| Entry DOI | 10.2210/pdb7wrg/pdb |
| Descriptor | Kinesin-like protein, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | kinesin, atpase, transport protein |
| Biological source | Caenorhabditis elegans |
| Total number of polymer chains | 2 |
| Total formula weight | 215554.14 |
| Authors | Wang, W.J.,Ren, J.Q.,Song, W.Y.,Feng, W. (deposition date: 2022-01-26, release date: 2022-08-10, Last modification date: 2023-11-29) |
| Primary citation | Wang, W.,Ren, J.,Song, W.,Zhang, Y.,Feng, W. The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition. Nat Commun, 13:4281-4281, 2022 Cited by PubMed Abstract: 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. PubMed: 35879313DOI: 10.1038/s41467-022-32048-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.16 Å) |
Structure validation
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