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TitleFlexible interwoven termini determine the thermal stability of thermosomes.
Journal, issue, pagesProtein Cell, Vol. 4, Issue 6, Page 432-444, Year 2013
Publish dateMay 25, 2013
AuthorsKai Zhang / Li Wang / Yanxin Liu / Kwok-Yan Chan / Xiaoyun Pang / Klaus Schulten / Zhiyang Dong / Fei Sun /
PubMed AbstractGroup 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 ...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-α and cpn-β), 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-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β 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.
External linksProtein Cell / PubMed:23709365 / PubMed Central
MethodsEM (single particle)
Resolution4.9 - 9.1 Å
Structure data

5391

3j1b

EMDB-5391: 8-fold symmetric rATcpn-alpha in apo state
PDB-3j1b: Cryo-EM structure of 8-fold symmetric rATcpn-alpha in apo state
Method: EM (single particle) / Resolution: 4.9 Å

5392

3j1c

EMDB-5392: 9-fold symmetric rATcpn-alpha in apo state
PDB-3j1c: Cryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state
Method: EM (single particle) / Resolution: 9.1 Å

5395

3j1e

EMDB-5395: 9-fold symmetric rATcpn-beta in apo state
PDB-3j1e: Cryo-EM structure of 9-fold symmetric rATcpn-beta in apo state
Method: EM (single particle) / Resolution: 8.3 Å

5396

3j1f

EMDB-5396: 9-fold symmetric rATcpn-beta in ATP-binding state
PDB-3j1f: Cryo-EM structure of 9-fold symmetric rATcpn-beta in ATP-binding state
Method: EM (single particle) / Resolution: 6.2 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • acidianus tengchongensis (archaea)
KeywordsCHAPERONE / Group II chaperonin

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