Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
- 등재 SCIE, SCOPUS
- 발행기관 Nature Publishing Group
- 발행년도 2017
- URI http://www.dcollection.net/handler/ewha/000000149640
- 본문언어 영어
- Published As http://dx.doi.org/10.1038/s41467-017-00980-z
초록/요약
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).
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