title: Structural changes underlying allostery in group II chaperonins.
abstract: The ATP-dependence of folding chamber closure in the 16-subunit homo-oligomeric chaperonin from archaea Methanococcus maripaludis (Mm-cpn) has been studied by single particle cryo-electron microscopy (Zhang et al., 2011). ATP binding alone causes a rigid body rotation of ~45° and slight closure of the cavity, but full closure requires ATP hydrolysis.
authors.affiliation: Section of Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London SW36JB, UK. keith.willison@icr.ac.uk
authors.forename: Keith R
authors.initials: KR
authors.lastname: Willison