论文信息 - Opening up the group II chaperonins.

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.

Zihe Rao

[1] M. Levitt,et al. Mechanism of Folding Chamber Closure in a Group II Chaperonin , 2010, Nature.

[2] Kai Zhang,et al. Crystal structure of group II chaperonin in the open state. , 2010, Structure.

[3] Masafumi Yohda,et al. Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms. , 2004, Journal of molecular biology.

[4] Paul D. Adams,et al. Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle*♦ , 2010, The Journal of Biological Chemistry.

[5] Robert Huber,et al. Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT , 1998, Cell.