9CRW
Crystal structure of the Candida albicans kinesin-8 proximal tail domain
Summary for 9CRW
| Entry DOI | 10.2210/pdb9crw/pdb |
| Descriptor | Kinesin-like protein (1 entity in total) |
| Functional Keywords | kinesin-8, microtubule, tail domain, tubulin, atpase, mitosis, mitotic spindle, stalk domain, motor protein |
| Biological source | Candida albicans |
| Total number of polymer chains | 8 |
| Total formula weight | 218374.53 |
| Authors | Trofimova, D.,Doubleday, C.,Hunter, B.,Serrano Arevalo, J.,Davison, E.,Wen, E.,Munro, K.,Allingham, J.S. (deposition date: 2024-07-22, release date: 2024-09-04, Last modification date: 2025-12-17) |
| Primary citation | Trofimova, D.,Doubleday, C.,Hunter, B.,Serrano Arevalo, J.D.,Davison, E.,Wen, E.,Munro, K.,Allingham, J.S. Fungal kinesin-8 motors dimerize by folding their proximal tail domain into a compact helical bundle. Structure, 33:2122-, 2025 Cited by PubMed Abstract: Kinesin-8 motors regulate kinetochore-microtubule dynamics and control spindle length and positioning. Certain isoforms achieve this by traversing microtubules, accumulating at plus-ends, and depolymerizing terminal αβ-tubulin subunits. While the kinesin-8 motor domain is well characterized, the tail domain regions are less understood. Using the Candida albicans Kip3 protein as a model for fungal kinesin-8, we present an X-ray crystal structure and hydrodynamic analysis of its motor-proximal tail segment, revealing its role in motor dimerization. This segment forms a compact, 92 Å-long four-helix bundle, rather than an elongated coiled-coil stalk seen in most kinesins. The bundle is stabilized primarily by interactions between helices one and three, with additional support from helices two and four. A flexible hinge bisects the bundle into two lobules, imparting mechanical pliability and asymmetric exterior surfaces. These unique features may facilitate interactions with regulatory elements or contribute to the functional versatility of kinesin-8 motors. PubMed: 40907488DOI: 10.1016/j.str.2025.08.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
Download full validation report
