Opening up the group II chaperonins.
A new study in this issue of Structure (Huo et al., 2010) reports the crystal structure of a group II chaperonin in the open state, providing unprecedented levels of detail for the domain movements that result from ATP hydrolysis and a clearer picture of the protein folding mechanism mediated by chaperonins.
Rao
Zihe
Z
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China. raozh@xtal.tsinghua.edu