3kfe

Crystal structures of a group II chaperonin from Methanococcus maripaludis

spinqualitylabelsall models 3kfe, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kfe is a 8 chain structure with sequence from methanococcus_deltae_corder_et_al._1988 Atcc 35294 methanococcus deltae corder et al. 1988. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, SO4 Related: 3kfb, 3kfk Gene: hsp60, MMP1515 (ATCC 35294 Methanococcus deltae Corder et al. 1988) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.,Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD J Biol Chem. 2010 Sep 3;285(36):27958-66. Epub 2010 Jun 23. PMID:20573955 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin 3D structures

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