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7Z56

Crystal Structure of the Ring Nuclease 0455 from Sulfolobus islandicus (Sis0455) in its apo form

これはPDB形式変換不可エントリーです。
7Z56 の概要
エントリーDOI10.2210/pdb7z56/pdb
関連するPDBエントリー7Z55
分子名称CRISPR-associated protein (2 entities in total)
機能のキーワードring nuclease, crispr-associated protein, antiviral protein, viral resistance, carf nucleotide-binding domain, crispr ring nuclease
由来する生物種Sulfolobus islandicus REY15A
タンパク質・核酸の鎖数2
化学式量合計47258.38
構造登録者
Molina, R.,Martin-Garcia, R.,Lopez-Mendez, B.,Jensen, A.L.G.,Marchena-Hurtado, J.,Stella, S.,Montoya, G. (登録日: 2022-03-08, 公開日: 2022-11-23, 最終更新日: 2024-10-16)
主引用文献Molina, R.,Garcia-Martin, R.,Lopez-Mendez, B.,Jensen, A.L.G.,Ciges-Tomas, J.R.,Marchena-Hurtado, J.,Stella, S.,Montoya, G.
Molecular basis of cyclic tetra-oligoadenylate processing by small standalone CRISPR-Cas ring nucleases.
Nucleic Acids Res., 50:11199-11213, 2022
Cited by
PubMed Abstract: Standalone ring nucleases are CRISPR ancillary proteins, which downregulate the immune response of Type III CRISPR-Cas systems by cleaving cyclic oligoadenylates (cA) second messengers. Two genes with this function have been found within the Sulfolobus islandicus (Sis) genome. They code for a long polypeptide composed by a CARF domain fused to an HTH domain and a short polypeptide constituted by a CARF domain with a 40 residue C-terminal insertion. Here, we determine the structure of the apo and substrate bound states of the Sis0455 enzyme, revealing an insertion at the C-terminal region of the CARF domain, which plays a key role closing the catalytic site upon substrate binding. Our analysis reveals the key residues of Sis0455 during cleavage and the coupling of the active site closing with their positioning to proceed with cA4 phosphodiester hydrolysis. A time course comparison of cA4 cleavage between the short, Sis0455, and long ring nucleases, Sis0811, shows the slower cleavage kinetics of the former, suggesting that the combination of these two types of enzymes with the same function in a genome could be an evolutionary strategy to regulate the levels of the second messenger in different infection scenarios.
PubMed: 36271789
DOI: 10.1093/nar/gkac923
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.27 Å)
構造検証レポート
Validation report summary of 7z56
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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