3KFB

Crystal structure of a group II chaperonin from Methanococcus maripaludis

Summary for 3KFB

• Entry DOI: 10.2210/pdb3kfb/pdb
• Related: 1a6d 1q3s 3KFE 3KFK
• Descriptor: Chaperonin, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total)
• Functional Keywords: double homo-octameric rings, atp-binding, chaperone, nucleotide-binding
• Biological source: Methanococcus maripaludis
• Total number of polymer chains: 8
• Total formula weight: 470566.10

Authors

Pereira, J.H.,Ralston, C.Y.,Douglas, N.,Meyer, D.,Knee, K.M.,Goulet, D.R.,King, J.A.,Frydman, J.,Adams, P.D. (deposition date: 2009-10-27, release date: 2010-06-23, Last modification date: 2011-07-13)

Primary citation

Pereira, J.H.,Ralston, C.Y.,Douglas, N.R.,Meyer, D.,Knee, K.M.,Goulet, D.R.,King, J.A.,Frydman, J.,Adams, P.D.
Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
J.Biol.Chem., 285:27958-27966, 2010

PubMed Abstract: Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we describe the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. In contrast with group I chaperonins, in which the equatorial domains share a similar conformation between the open and closed states and the largest motions occurs at the intermediate and apical domains, the three domains of the archaeal chaperonin subunit reorient as a single rigid body. The large rotation observed from the open state to the closed state results in a 65% decrease of the folding chamber volume and creates a highly hydrophilic surface inside the cage. These results suggest a completely distinct closing mechanism in the group II chaperonins as compared with the group I chaperonins.

PubMed: 20573955
DOI: 10.1074/jbc.M110.125344

Experimental method

X-RAY DIFFRACTION (3.2 Å)