6GZC

heterotetrameric katanin p60:p80 complex

Summary for 6GZC

• Entry DOI: 10.2210/pdb6gzc/pdb
• Descriptor: Katanin p80 WD40 repeat-containing subunit B1, Katanin p60 ATPase-containing subunit A1, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: katanin, severing enzyme, microtubule, cytoskeleton, hydrolase
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 65820.07

Authors

Faltova, L.,Jiang, K.,Frey, D.,Wu, Y.,Capitani, G.,Prota, A.E.,Akhmanova, A.,Steinmetz, M.O.,Kammerer, R.A. (deposition date: 2018-07-03, release date: 2019-08-07, Last modification date: 2024-01-17)

Primary citation

Faltova, L.,Jiang, K.,Frey, D.,Wu, Y.,Capitani, G.,Prota, A.E.,Akhmanova, A.,Steinmetz, M.O.,Kammerer, R.A.
Crystal Structure of a Heterotetrameric Katanin p60:p80 Complex.
Structure, 27:1375-1383.e3, 2019

PubMed Abstract: Katanin is a microtubule-severing enzyme that is crucial for many cellular processes. Katanin consists of two subunits, p60 and p80, that form a stable complex. The interaction between subunits is mediated by the p60 N-terminal microtubule-interacting and -trafficking domain (p60-MIT) and the p80 C-terminal domain (p80-CTD). Here, we performed a biophysical characterization of the mouse p60-MIT:p80-CTD heterodimer and show that this complex can assemble into heterotetramers. We identified two mutations that enhance heterotetramer formation and determined the X-ray crystal structure of this mutant complex. The structure revealed a domain-swapped heterotetramer consisting of two p60-MIT:p80-CTD heterodimers. Structure-based sequence alignments suggest that heterotetramerization of katanin might be a common feature of various species. Furthermore, we show that enhanced heterotetramerization of katanin impairs its microtubule end-binding properties and increases the enzyme's microtubule lattice binding and severing activities. Therefore, our findings suggest the existence of different katanin oligomers that possess distinct functional properties.

PubMed: 31353241
DOI: 10.1016/j.str.2019.07.002

Experimental method

X-RAY DIFFRACTION (2 Å)