Literature summary for 5.6.1.1 extracted from

Rezabkova, L.; Jiang, K.; Capitani, G.; Prota, A.E.; Akhmanova, A.; Steinmetz, M.O.; Kammerer, R.A.
Structural basis of katanin p60 p80 complex formation (2017), Sci. Rep., 7, 14893 .

Search for more literature for 5.6.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
mouse p80-CTD (residues 481-658) are cloned into a modified version of the pET-15b vector, pHisTrx2, which includes Escherichia coli thioredoxin A as a fusion protein after the His6 tag	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
high-resolution structure of the heterodimeric complex of p60-microtubule interacting and trafficking domain and the p80 C-terminal domain is determined by X-ray crystallography	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9WV86 AND Q8BG40	Q9WV86: p60 ATPase-containing subunit, Q8BG40: p80 subunit	-

Subunits

Subunits	Comment	Organism
?	the enzyme consists two subunits, the catalytic p60 subunit and the p80 subunit. ADP-bound p60 is typically monomeric and exchange of ADP to ATP induces hexamerization. The hexameric p60 subunit is active alone, its association with the p80 subunit greatly enhances both the microtubule-binding and microtubule-severing activities of katanin. The interaction between the two katanin subunits is mediated by the p60-MIT domain and the p80 C-terminal domain	Mus musculus

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Release 2023.1 (January 2023)