Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
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Title
- Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium
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Author(s)
- An, Young Jun; Rowland, Sara E.; Na, Jung-Hyun; Spigolon, Dario; Hong, Seung Kon; Yoon, Yeo Joon; Lee, Jung-Hyun; Robb, Frank T.; Cha, Sun-Shin
- KIOST Author(s)
- An, Young Jun(안영준); Lee, Jung Hyun(이정현)
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Alternative Author(s)
- 안영준; 이정현
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Publication Year
- 2017-10-10
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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.
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ISSN
- 2041-1723
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/1134
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DOI
- 10.1038/s41467-017-00980-z
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Bibliographic Citation
- NATURE COMMUNICATIONS, v.8, 2017
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Publisher
- NATURE PUBLISHING GROUP
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Subject
- GROUP-II CHAPERONIN; CYTOPLASMIC CHAPERONIN; MOLECULAR CHAPERONE; CRYSTAL-STRUCTURE; HEAT-SHOCK; COMPLEX; BINDING; SYSTEMS; DOMAIN; PREFOLDIN
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Type
- Article
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Language
- English
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Document Type
- Article
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