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TitleCryo-EM structures of GroEL:ES with RuBisCO visualize molecular contacts of encapsulated substrates in a double-cage chaperonin.
Journal, issue, pagesiScience, Vol. 25, Issue 1, Page 103704, Year 2022
Publish dateJan 21, 2022
AuthorsHyunmin Kim / Junsun Park / Seyeon Lim / Sung-Hoon Jun / Mingyu Jung / Soung-Hun Roh /
PubMed AbstractThe 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.
External linksiScience / PubMed:35036883 / PubMed Central
MethodsEM (single particle)
Resolution7.6 Å
Structure data

32164

7vwx

EMDB-32164, PDB-7vwx:
CryoEM structure of football-shaped GroEL:ES2 with RuBisCO
Method: EM (single particle) / Resolution: 7.6 Å

Source
  • escherichia coli k-12 (bacteria)
  • rhodospirillum rubrum atcc 11170 (bacteria)
KeywordsCHAPERONE / GroEL/ES system / substrate folding / folding assistance

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