2RPA
The solution structure of N-terminal domain of microtubule severing enzyme
Summary for 2RPA
| Entry DOI | 10.2210/pdb2rpa/pdb |
| Descriptor | Katanin p60 ATPase-containing subunit A1 (1 entity in total) |
| Functional Keywords | aaa atpase, atp-binding, cell cycle, cell division, cytoplasm, hydrolase, microtubule, microtubule severing enzyme, mitosis, nucleotide-binding |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cytoplasm (By similarity): Q9WV86 |
| Total number of polymer chains | 1 |
| Total formula weight | 9256.64 |
| Authors | Iwaya, N.,Kuwahara, Y.,Unzai, S.,Nagata, T.,Tomii, K.,Goda, N.,Tochio, H.,Shirakawa, M.,Hiroaki, H. (deposition date: 2008-05-13, release date: 2009-05-26, Last modification date: 2024-05-29) |
| Primary citation | Iwaya, N.,Kuwahara, Y.,Fujiwara, Y.,Goda, N.,Tenno, T.,Akiyama, K.,Mase, S.,Tochio, H.,Ikegami, T.,Shirakawa, M.,Hiroaki, H. A common substrate recognition mode conserved between katanin P60 and VPS4 governs microtubule severing and membrane skeleton reorganization J.Biol.Chem., 285:16822-16829, 2010 Cited by PubMed Abstract: Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD was determined by NMR. Although their sequence similarities were as low as 20%, the structure of kp60-NTD revealed a striking similarity to those of the microtubule interacting and trafficking (MIT) domains, which adopt anti-parallel three-stranded helix bundle. In particular, the arrangement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, which is a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. Mutation studies revealed that the positively charged surface formed by helices 2 and 3 binds tubulin. This binding mode resembles the interaction between the MIT domain of Vps4 and Vps2/CHMP1a, a component of endosomal sorting complexes required for transport III. Our results show that both the molecular architecture and the binding modes are conserved between two AAA-ATPases, kp60 and Vps4. A common mechanism is evolutionarily conserved between two distinct cellular events, one that drives microtubule severing and the other involving membrane skeletal reorganization. PubMed: 20339000DOI: 10.1074/jbc.M110.108365 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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