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-Structure paper
タイトル | Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy. |
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ジャーナル・号・ページ | Acta Crystallogr F Struct Biol Commun, Vol. 77, Issue Pt 3, Page 79-84, Year 2021 |
掲載日 | 2021年3月1日 |
著者 | Yi Cheng Zeng / Meghna Sobti / Alastair G Stewart / |
PubMed 要旨 | Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. ...Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. Using cryo-electron microscopy, structures of the β-only complex of S. solfataricus TF55 (TF55β) were determined to 3.6-4.2 Å resolution. The structures of the TF55β complexes formed in the presence of ADP or ATP highlighted an open state in which nucleotide exchange can occur before progressing in the refolding cycle. |
リンク | Acta Crystallogr F Struct Biol Commun / PubMed:33682792 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.62 - 5.22 Å |
構造データ | EMDB-21211: EMDB-22186, PDB-6xhi: EMDB-22187, PDB-6xhj: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-ATP: |
由来 |
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キーワード | CHAPERONE / Chaperonin / Complex |