5NBT
Apo structure of p60N/p80C katanin
Summary for 5NBT
| Entry DOI | 10.2210/pdb5nbt/pdb |
| Descriptor | Katanin p80 WD40 repeat-containing subunit B1, Katanin p60 ATPase-containing subunit A1 (3 entities in total) |
| Functional Keywords | katanin, severing enzyme, microtubule, cytoskeleton, hydrolase |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Cytoplasm : Q8BG40 Q9WV86 |
| Total number of polymer chains | 4 |
| Total formula weight | 65740.05 |
| Authors | Jiang, K.,Rezabkova, L.,Hua, S.,Liu, Q.,Capitani, G.,Altelaar, A.F.M.,Heck, A.J.R.,Kammerer, R.A.,Steinmetz, M.O.,Akhmanova, A. (deposition date: 2017-03-02, release date: 2017-04-26, Last modification date: 2024-05-08) |
| Primary citation | Jiang, K.,Rezabkova, L.,Hua, S.,Liu, Q.,Capitani, G.,Maarten Altelaar, A.F.,Heck, A.J.R.,Kammerer, R.A.,Steinmetz, M.O.,Akhmanova, A. Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex. Nat. Cell Biol., 19:480-492, 2017 Cited by PubMed Abstract: ASPM (known as Asp in fly and ASPM-1 in worm) is a microcephaly-associated protein family that regulates spindle architecture, but the underlying mechanism is poorly understood. Here, we show that ASPM forms a complex with another protein linked to microcephaly, the microtubule-severing ATPase katanin. ASPM and katanin localize to spindle poles in a mutually dependent manner and regulate spindle flux. X-ray crystallography revealed that the heterodimer formed by the N- and C-terminal domains of the katanin subunits p60 and p80, respectively, binds conserved motifs in ASPM. Reconstitution experiments demonstrated that ASPM autonomously tracks growing microtubule minus ends and inhibits their growth, while katanin decorates and bends both ends of dynamic microtubules and potentiates the minus-end blocking activity of ASPM. ASPM also binds along microtubules, recruits katanin and promotes katanin-mediated severing of dynamic microtubules. We propose that the ASPM-katanin complex controls microtubule disassembly at spindle poles and that misregulation of this process can lead to microcephaly. PubMed: 28436967DOI: 10.1038/ncb3511 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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