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-Structure paper
タイトル | Novel cryo-EM structure of an ADP-bound GroEL-GroES complex. |
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ジャーナル・号・ページ | Sci Rep, Vol. 11, Issue 1, Page 18241, Year 2021 |
掲載日 | 2021年9月14日 |
著者 | 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 / |
PubMed 要旨 | 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 ...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. |
リンク | Sci Rep / PubMed:34521893 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.4 - 3.43 Å |
構造データ | EMDB-13293, PDB-7pbj: EMDB-13308, PDB-7pbx: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-HOH: |
由来 |
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キーワード | CHAPERONE / cryo-EM / chaperonin / GroEL / GroEL-GroES |