3KFE
Crystal structures of a group II chaperonin from Methanococcus maripaludis
Summary for 3KFE
Entry DOI | 10.2210/pdb3kfe/pdb |
Related | 3KFB 3KFK |
Descriptor | Chaperonin, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 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 | 449293.65 |
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: 2024-10-30) |
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 Cited by 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: 20573955DOI: 10.1074/jbc.M110.125344 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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