PDBsum entry 6b5c

Cell cycle

PDB id: 6b5c

Contents

Protein chain

293 a.a.

Ligands

PG4

Waters ×53

PDB id:

6b5c

Name:

Cell cycle

Title:

Structural basis for katanin self-assembly

Structure:

Katanin p60 atpase-containing subunit a-like 1. Chain: a. Synonym: katanin p60 subunit a-like 1,p60 katanin-like 1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: katnal1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.40Å R-factor: 0.217 R-free: 0.253

Authors:

S.Nithianantham,J.Al-Bassam

Key ref:

S.Nithianantham et al. (2018). Structural basis for disassembly of katanin heterododecamers. J Biol Chem, 293, 10590-10605. PubMed id: 29752405

Date:

29-Sep-17 Release date: 23-May-18

Protein chain

Q9BW62  (KATL1_HUMAN) -  Katanin p60 ATPase-containing subunit A-like 1 from Homo sapiens

Seq: 490 a.a.

Struc: 293 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.5.6.1.1 - microtubule-severing ATPase.
• Reaction: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Biol Chem 293:10590-10605 (2018)

PubMed id: 29752405

Structural basis for disassembly of katanin heterododecamers.

S.Nithianantham, F.J.McNally, J.Al-Bassam.

ABSTRACT

The reorganization of microtubules in mitosis, meiosis, and development requires the microtubule-severing activity of katanin. Katanin is a heterodimer composed of an ATPase associated with diverse cellular activities (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.