7PBJ

Cryo-EM structure of the GroEL-GroES complex with ADP bound to both rings ("wide" conformation).

This is a non-PDB format compatible entry.

Summary for 7PBJ

• Entry DOI: 10.2210/pdb7pbj/pdb
• EMDB information: 13293
• Descriptor: 60 kDa chaperonin, 10 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: cryo-em, chaperonin, groel, groel-groes, chaperone
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 21
• Total formula weight: 852209.12

Authors

Pichkur, E.B.,Stanishneva-Konovalova, T.B. (deposition date: 2021-08-02, release date: 2021-11-24, Last modification date: 2024-07-17)

Primary citation

Kudryavtseva, S.S.,Pichkur, E.B.,Yaroshevich, I.A.,Mamchur, A.A.,Panina, I.S.,Moiseenko, A.V.,Sokolova, O.S.,Muronetz, V.I.,Stanishneva-Konovalova, T.B.
Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.
Sci Rep, 11:18241-18241, 2021

PubMed Abstract: The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL-GroES complex at 3.4 Å resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATP:ADP ratios.

PubMed: 34521893
DOI: 10.1038/s41598-021-97657-x

Experimental method

ELECTRON MICROSCOPY (3.4 Å)