6EXP
Crystal structure of the SIRV3 AcrID1 (gp02) anti-CRISPR protein
6EXP の概要
| エントリーDOI | 10.2210/pdb6exp/pdb |
| 分子名称 | SIRV3 AcrID1 (gp02) anti-CRISPR protein (2 entities in total) |
| 機能のキーワード | anti-crispr, crispr-cas, sulfolobus islandicus rod shaped virus 2, inhibitor, sirv3, viral protein |
| 由来する生物種 | Sulfolobus islandicus rudivirus 3 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 78520.16 |
| 構造登録者 | He, F.,Bhoobalan-Chitty, Y.,Van, L.B.,Kjeldsen, A.L.,Dedola, M.,Makarova, K.S.,Koonin, E.V.,Brodersen, D.E.,Peng, X. (登録日: 2017-11-08, 公開日: 2018-01-31, 最終更新日: 2024-05-08) |
| 主引用文献 | He, F.,Bhoobalan-Chitty, Y.,Van, L.B.,Kjeldsen, A.L.,Dedola, M.,Makarova, K.S.,Koonin, E.V.,Brodersen, D.E.,Peng, X. Anti-CRISPR proteins encoded by archaeal lytic viruses inhibit subtype I-D immunity. Nat Microbiol, 3:461-469, 2018 Cited by PubMed Abstract: Viruses employ a range of strategies to counteract the prokaryotic adaptive immune system, clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas), including mutational escape and physical blocking of enzymatic function using anti-CRISPR proteins (Acrs). Acrs have been found in many bacteriophages but so far not in archaeal viruses, despite the near ubiquity of CRISPR-Cas systems in archaea. Here, we report the functional and structural characterization of two archaeal Acrs from the lytic rudiviruses, SIRV2 and SIRV3. We show that a 4 kb deletion in the SIRV2 genome dramatically reduces infectivity in Sulfolobus islandicus LAL14/1 that carries functional CRISPR-Cas subtypes I-A, I-D and III-B. Subsequent insertion of a single gene from SIRV3, gp02 (AcrID1), which is conserved in the deleted fragment, successfully restored infectivity. We demonstrate that AcrID1 protein inhibits the CRISPR-Cas subtype I-D system by interacting directly with Cas10d protein, which is required for the interference stage. Sequence and structural analysis of AcrID1 show that it belongs to a conserved family of compact, dimeric αβ-sandwich proteins characterized by extreme pH and temperature stability and a tendency to form protein fibres. We identify about 50 homologues of AcrID1 in four archaeal viral families demonstrating the broad distribution of this group of anti-CRISPR proteins. PubMed: 29507349DOI: 10.1038/s41564-018-0120-z 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.93 Å) |
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