Structural highlights
Publication Abstract from PubMedChaperonins 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, ATPgammaS-, and ADP-bound states, with a resolution of 4.3A, 5.0A, and 6A, respectively. The structure of OBP chaperonin reveals a unique subunit arrangement, with three subunits pairs and one unpaired subunit. Each pair combines subunits in two possible conformations, differing in nucleotide-binding affinity. Binding of nucleotides result in the increase of subunits' conformational variability. Due to its unique structural and functional features, OBP chaperonin can represent a new group. 148 words. Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin.,Stanishneva-Konovalova TB, Semenyuk PI, Kurochkina LP, Pichkur EB, Vasilyev AL, Kovalchuk MV, Kirpichnikov MP, Sokolova OS J Struct Biol. 2019 Dec 20:107439. doi: 10.1016/j.jsb.2019.107439. PMID:31870903[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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