6B5C

Structural Basis for Katanin Self-Assembly

Summary for 6B5C

• Entry DOI: 10.2210/pdb6b5c/pdb
• Descriptor: Katanin p60 ATPase-containing subunit A-like 1, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: katanin, aaa atpase, microtubule severing protein, cell cycle
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 34817.11

Authors

Nithianantham, S.,Al-Bassam, J. (deposition date: 2017-09-29, release date: 2018-05-23, Last modification date: 2023-10-04)

Primary citation

Nithianantham, S.,McNally, F.J.,Al-Bassam, J.
Structural basis for disassembly of katanin heterododecamers.
J. Biol. Chem., 293:10590-10605, 2018

PubMed Abstract: The reorganization of microtubules in mitosis, meiosis, and development requires the microtubule-severing activity of katanin. Katanin is a heterodimer composed of an TPase ssociated with diverse cellular ctivities (AAA) subunit and a regulatory subunit. Microtubule severing requires ATP hydrolysis by katanin's conserved AAA ATPase domains. Whereas other AAA ATPases form stable hexamers, we show that katanin forms only a monomer or dimers of heterodimers in solution. Katanin oligomers consistent with hexamers of heterodimers or heterododecamers were only observed for an ATP hydrolysis-deficient mutant in the presence of ATP. X-ray structures of katanin's AAA ATPase in monomeric nucleotide-free and pseudo-oligomeric ADP-bound states revealed conformational changes in the AAA subdomains that explained the structural basis for the instability of the katanin heterododecamer. We propose that the rapid dissociation of katanin AAA oligomers may lead to an autoinhibited state that prevents inappropriate microtubule severing or that cyclical disassembly into heterodimers may critically contribute to the microtubule-severing mechanism.

PubMed: 29752405
DOI: 10.1074/jbc.RA117.001215

Experimental method

X-RAY DIFFRACTION (2.4 Å)