Novel cryo-EM structure of an ADP-bound GroEL–GroES complex
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 conformationa...
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2021
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oai:doaj.org-article:accfa7162fbd4527a18ab1b47e2289062021-12-02T18:33:47ZNovel cryo-EM structure of an ADP-bound GroEL–GroES complex10.1038/s41598-021-97657-x2045-2322https://doaj.org/article/accfa7162fbd4527a18ab1b47e2289062021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-97657-xhttps://doaj.org/toc/2045-2322Abstract 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–GroES1 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.Sofia S. KudryavtsevaEvgeny B. PichkurIgor A. YaroshevichAleksandra A. MamchurIrina S. PaninaAndrei V. MoiseenkoOlga S. SokolovaVladimir I. MuronetzTatiana B. Stanishneva-KonovalovaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021) |
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Medicine R Science Q Sofia S. Kudryavtseva Evgeny B. Pichkur Igor A. Yaroshevich Aleksandra A. Mamchur Irina S. Panina Andrei V. Moiseenko Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
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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–GroES1 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. |
format |
article |
author |
Sofia S. Kudryavtseva Evgeny B. Pichkur Igor A. Yaroshevich Aleksandra A. Mamchur Irina S. Panina Andrei V. Moiseenko Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova |
author_facet |
Sofia S. Kudryavtseva Evgeny B. Pichkur Igor A. Yaroshevich Aleksandra A. Mamchur Irina S. Panina Andrei V. Moiseenko Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova |
author_sort |
Sofia S. Kudryavtseva |
title |
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
title_short |
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
title_full |
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
title_fullStr |
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
title_full_unstemmed |
Novel cryo-EM structure of an ADP-bound GroEL–GroES complex |
title_sort |
novel cryo-em structure of an adp-bound groel–groes complex |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/accfa7162fbd4527a18ab1b47e228906 |
work_keys_str_mv |
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