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Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium

Title
Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
Authors
An Y.J.Rowland S.E.Na J.-H.Spigolon D.Hong S.K.Yoon Y.J.Lee J.-H.Robb F.T.Cha S.-S.
Ewha Authors
윤여준차선신
SCOPUS Author ID
윤여준scopus; 차선신scopus
Issue Date
2017
Journal Title
Nature Communications
ISSN
2041-1723JCR Link
Citation
vol. 8, no. 1
Publisher
Nature Publishing Group
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The chaperonins (CPNs) are megadalton sized hollow complexes with two cavities that open and close to encapsulate non-native proteins. CPNs are assigned to two sequence-related groups that have distinct allosteric mechanisms. In Group I CPNs a detachable co-chaperone, GroES, closes the chambers whereas in Group II a built-in lid closes the chambers. Group I CPNs have a bacterial ancestry, whereas Group II CPNs are archaeal in origin. Here we describe open and closed crystal structures representing a new phylogenetic branch of CPNs. These Group III CPNs are divergent in sequence and structure from extant CPNs, but are closed by a built-in lid like Group II CPNs. A nucleotide-sensing loop, present in both Group I and Group II CPNs, is notably absent. We identified inter-ring pivot joints that articulate during ring closure. These Group III CPNs likely represent a relic from the ancestral CPN that formed distinct bacterial and archaeal branches. © 2017 The Author(s).
DOI
10.1038/s41467-017-00980-z
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자연과학대학 > 화학·나노과학전공 > Journal papers
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