+検索条件
-Structure paper
タイトル | Cryo-EM structures of GroEL:ES with RuBisCO visualize molecular contacts of encapsulated substrates in a double-cage chaperonin. |
---|---|
ジャーナル・号・ページ | iScience, Vol. 25, Issue 1, Page 103704, Year 2022 |
掲載日 | 2022年1月21日 |
著者 | Hyunmin Kim / Junsun Park / Seyeon Lim / Sung-Hoon Jun / Mingyu Jung / Soung-Hun Roh / |
PubMed 要旨 | The GroEL/GroES chaperonin system assists the folding of many proteins, through conformational transitions driven by ATP hydrolysis. Although structural information about bullet-shaped GroEL:ES ...The GroEL/GroES chaperonin system assists the folding of many proteins, through conformational transitions driven by ATP hydrolysis. Although structural information about bullet-shaped GroEL:ES complexes has been extensively reported, the substrate interactions of another functional complex, the football-shaped GroEL:ES, remain elusive. Here, we report single-particle cryo-EM structures of reconstituted wild-type GroEL:ES complexes with a chemically denatured substrate, ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO). Our structures demonstrate that native-like folded RuBisCO density is captured at the lower part of the GroEL chamber and that GroEL's bulky hydrophobic residues Phe281, Tyr360, and Phe44 contribute to direct contact with RuBisCO density. In addition, our analysis found that GroEL:ES can be occupied by two substrates simultaneously, one in each chamber. Together, these observations provide insights to the football-shaped GroEL:ES complex as a functional state to assist the substrate folding with visualization. |
リンク | iScience / PubMed:35036883 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 7.6 Å |
構造データ | EMDB-32164, PDB-7vwx: |
由来 |
|
キーワード | CHAPERONE / GroEL/ES system / substrate folding / folding assistance |