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8OZF

cryoEM structure of SPARTA complex Tetramer Post-NAD cleavage-2

これはPDB形式変換不可エントリーです。
8OZF の概要
エントリーDOI10.2210/pdb8ozf/pdb
EMDBエントリー17305 17307
分子名称TIR domain-containing protein, Piwi domain-containing protein, RNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3'), ... (5 entities in total)
機能のキーワードsparta, tir, prokaryotic argonaute, antiviral protein
由来する生物種Maribacter polysiphoniae
詳細
タンパク質・核酸の鎖数16
化学式量合計488296.16
構造登録者
Babatunde, E.,Dong, C.N.,Xu, H.L.,Henning, S. (登録日: 2023-05-09, 公開日: 2023-08-16, 最終更新日: 2023-08-23)
主引用文献Ni, D.,Lu, X.,Stahlberg, H.,Ekundayo, B.
Activation mechanism of a short argonaute-TIR prokaryotic immune system.
Sci Adv, 9:eadh9002-eadh9002, 2023
Cited by
PubMed Abstract: Short prokaryotic argonaute (pAgo) and toll/interleukin-1 receptor/resistance protein (TIR)-analog of PAZ (APAZ) form a heterodimeric SPARTA complex that provides immunity to its prokaryotic host through an abortive infection mechanism. Monomeric SPARTA senses foreign RNA/DNA duplexes to assemble an active tetramer resulting in cell death by nicotinamide adenine dinucleotide (oxidized form) (NAD) depletion via an unknown mechanism. We report nine structures of SPARTA in different functional states at a resolution range of 4.2 to 2.9 angstroms, revealing its activation mechanism. Inactive SPARTA monomers bind to RNA/DNA duplexes to form symmetric dimers mediated by the association of Ago subunits. The initiation of tetramer assembly induces flexibility of the TIR domains enabling a symmetry-breaking rotational movement of a TIR domain in the dimer units which facilitates the TIR oligomerization, resulting in the formation of the substrate binding pocket and the activation of the SPARTA complex's NADase activity. Our findings provide detailed structural and mechanistic insights into activating a short argonaute defense system.
PubMed: 37467330
DOI: 10.1126/sciadv.adh9002
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.73 Å)
構造検証レポート
Validation report summary of 8ozf
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2024-11-13に公開中

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