5ZQL
crystal structure of human katanin AAA ATPase domain
Summary for 5ZQL
| Entry DOI | 10.2210/pdb5zql/pdb |
| Descriptor | Katanin p60 ATPase-containing subunit A1 (1 entity in total) |
| Functional Keywords | katanin p60, aaa atpase, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 70130.43 |
| Authors | Kim, E.E.,Shin, S.C. (deposition date: 2018-04-19, release date: 2019-02-27, Last modification date: 2023-11-22) |
| Primary citation | Shin, S.C.,Im, S.K.,Jang, E.H.,Jin, K.S.,Hur, E.M.,Kim, E.E. Structural and Molecular Basis for Katanin-Mediated Severing of Glutamylated Microtubules. Cell Rep, 26:1357-1367.e5, 2019 Cited by PubMed Abstract: Katanin was the first microtubule (MT)-severing enzyme discovered, but how katanin executes MT severing remains poorly understood. Here, we report X-ray crystal structures of the apo and ATPγS-bound states of the catalytic AAA domain of human katanin p60 at 3.0 and 2.9 Å resolution, respectively. Comparison of the two structures reveals conformational changes induced by ATP binding and how such changes ensure hexamer stability. Moreover, we uncover structural details of pore loops (PLs) and show that Arg283, a residue unique to katanin among MT-severing enzymes, protrudes from PL1 and lines the entry of the catalytic pore. Functional studies suggest that PL1 and Arg283 play essential roles in the recognition and remodeling of the glutamylated, C-terminal tubulin tail and regulation of axon growth. In addition, domain-swapping experiments in katanin and spastin suggest that the non-homologous N-terminal region, which contains the MT-interacting and trafficking domain and a linker, confers specificity to the severing process. PubMed: 30699360DOI: 10.1016/j.celrep.2019.01.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.007 Å) |
Structure validation
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