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TitleCryo-EM reveals an asymmetry in a novel single-ring viral chaperonin.
Journal, issue, pagesJ Struct Biol, Vol. 209, Issue 2, Page 107439, Year 2020
Publish dateFeb 1, 2020
AuthorsTatiana B Stanishneva-Konovalova / Pavel I Semenyuk / Lidia P Kurochkina / Evgeny B Pichkur / Alexander L Vasilyev / Mikhail V Kovalchuk / Mikhail P Kirpichnikov / Olga S Sokolova /
PubMed AbstractChaperonins are ubiquitously present protein complexes, which assist the proper folding of newly synthesized proteins and prevent aggregation of denatured proteins in an ATP-dependent manner. They ...Chaperonins are ubiquitously present protein complexes, which assist the proper folding of newly synthesized proteins and prevent aggregation of denatured proteins in an ATP-dependent manner. They are classified into group I (bacterial, mitochondrial, chloroplast chaperonins) and group II (archaeal and eukaryotic cytosolic variants). However, both of these groups do not include recently discovered viral chaperonins. Here, we solved the symmetry-free cryo-EM structures of a single-ring chaperonin encoded by the gene 246 of bacteriophage OBP Pseudomonas fluorescens, in the nucleotide-free, ATPγS-, and ADP-bound states, with resolutions of 4.3 Å, 5.0 Å, and 6 Å, respectively. The structure of OBP chaperonin reveals a unique subunit arrangement, with three pairs of subunits and one unpaired subunit. Each pair combines subunits in two possible conformations, differing in nucleotide-binding affinity. The binding of nucleotides results in the increase of subunits' conformational variability. Due to its unique structural and functional features, OBP chaperonin can represent a new group.
External linksJ Struct Biol / PubMed:31870903
MethodsEM (single particle)
Resolution4.5 - 6.5 Å
Structure data

EMDB-0191:
OBP chaperonin in the ADP-bound state
Method: EM (single particle) / Resolution: 6.5 Å

0204

6hdd

EMDB-0204, PDB-6hdd:
OBP chaperonin in the nucleotide-free state
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-0208:
OBP chaperonin in the ATPgammaS-bound state
Method: EM (single particle) / Resolution: 5.0 Å

Source
  • pseudomonas phage obp (virus)
KeywordsCHAPERONE / chaperonin / nucleotide-free

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