Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.

Autor: Kudryavtseva SS; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia.; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Pichkur EB; National Research Center «Kurchatov Institute», Moscow, Russia.; Petersburg Nuclear Physics Institute Named by B.P. Konstantinov of NRC «Kurchatov Institute», 1, Orlova Roshcha, Gatchina, Russia, 188300., Yaroshevich IA; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia., Mamchur AA; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia., Panina IS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia., Moiseenko AV; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia., Sokolova OS; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia., Muronetz VI; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia., Stanishneva-Konovalova TB; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia. stanishneva-konovalova@mail.bio.msu.ru.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2021 Sep 14; Vol. 11 (1), pp. 18241. Date of Electronic Publication: 2021 Sep 14.
DOI: 10.1038/s41598-021-97657-x
Abstrakt: 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 1 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.
(© 2021. The Author(s).)
Databáze: MEDLINE
Externí odkaz: