3j1e | pdb_00003j1e

Cryo-EM structure of 9-fold symmetric rATcpn-beta in apo state

spinqualitylabelsall models 3j1e, resolution 8.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j1e is a 18 chain structure with sequence from "acidianus_tengchongenses"_he_et_al._2001 "acidianus tengchongenses" he et al. 2001. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3j1b, 3j1c, 3j1d, 3j1f, 3j1g, 3j1h, 3j1i, 3j1j, 3j1k, 3j1l Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-alpha and cpn-beta), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-beta is more thermally stable than cpn-alpha, while the thermal stability of the hetero thermosome cpn-alphabeta is intermediate. Cryo-electron microscopy reconstructions of cpn-alpha and cpn-beta revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes. Flexible interwoven termini determine the thermal stability of thermosomes.,Zhang K, Wang L, Liu Y, Chan KY, Pang X, Schulten K, Dong Z, Sun F Protein Cell. 2013 Jun;4(6):432-44. doi: 10.1007/s13238-013-3026-9. Epub 2013 May, 25. PMID:23709365 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin

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