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

• Published in: Nature communications Vol. 8; no. 1; pp. 827 - 11
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.10.2017; Nature Publishing Group; Nature Portfolio
• Subjects: 631/45/535/1266/1265; 631/92/603; Adenosine triphosphate; Allosteric properties; Bacteria; Chambers; Chaperonins; Crystal structure; Folding machines; Humanities and Social Sciences; multidisciplinary; Phylogeny; Protein folding; Proteins; Science; Science (multidisciplinary); Structural analysis

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 wher...