4UBF
HsMCAK motor domain complex
Summary for 4UBF
| Entry DOI | 10.2210/pdb4ubf/pdb |
| Descriptor | Kinesin-like protein KIF2C, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | mcak, kif2c, complex, motor domain, cell cycle |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 176437.80 |
| Authors | Welburn, J.P.I.,Talapatra, S.K. (deposition date: 2014-08-12, release date: 2015-05-06, Last modification date: 2023-12-20) |
| Primary citation | Talapatra, S.K.,Harker, B.,Welburn, J.P. The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch. Elife, 4:-, 2015 Cited by PubMed Abstract: The precise regulation of microtubule dynamics is essential during cell division. The kinesin-13 motor protein MCAK is a potent microtubule depolymerase. The divergent non-motor regions flanking the ATPase domain are critical in regulating its targeting and activity. However, the molecular basis for the function of the non-motor regions within the context of full-length MCAK is unknown. Here, we determine the structure of MCAK motor domain bound to its regulatory C-terminus. Our analysis reveals that the MCAK C-terminus binds to two motor domains in solution and is displaced allosterically upon microtubule binding, which allows its robust accumulation at microtubule ends. These results demonstrate that MCAK undergoes long-range conformational changes involving its C-terminus during the soluble to microtubule-bound transition and that the C-terminus-motor interaction represents a structural intermediate in the MCAK catalytic cycle. Together, our work reveals intrinsic molecular mechanisms underlying the regulation of kinesin-13 activity. PubMed: 25915621DOI: 10.7554/eLife.06421 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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