8UAE

E. coli Sir2_HerA complex (12:6) with ATPgamaS

これはPDB形式変換不可エントリーです。

8UAE の概要

• エントリーDOI: 10.2210/pdb8uae/pdb
• EMDBエントリー: 42061
• 分子名称: SIR2-like domain-containing protein, Nucleoside triphosphate hydrolase, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: hera, sir2, nadase, atpase, anti-phage system, immune system
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 981853.47

構造登録者

Shen, Z.F.,Lin, Q.P.,Fu, T.M. (登録日: 2023-09-20, 公開日: 2023-12-27, 最終更新日: 2024-03-27)

主引用文献

Shen, Z.,Lin, Q.,Yang, X.Y.,Fosuah, E.,Fu, T.M.
Assembly-mediated activation of the SIR2-HerA supramolecular complex for anti-phage defense.
Mol.Cell, 83:4586-4599.e5, 2023

PubMed Abstract: SIR2-HerA, a bacterial two-protein anti-phage defense system, induces bacterial death by depleting NAD upon phage infection. Biochemical reconstitution of SIR2, HerA, and the SIR2-HerA complex reveals a dynamic assembly process. Unlike other ATPases, HerA can form various oligomers, ranging from dimers to nonamers. When assembled with SIR2, HerA forms a hexamer and converts SIR2 from a nuclease to an NAD hydrolase, representing an unexpected regulatory mechanism mediated by protein assembly. Furthermore, high concentrations of ATP can inhibit NAD hydrolysis by the SIR2-HerA complex. Cryo-EM structures of the SIR2-HerA complex reveal a giant supramolecular assembly up to 1 MDa, with SIR2 as a dodecamer and HerA as a hexamer, crucial for anti-phage defense. Unexpectedly, the HerA hexamer resembles a spiral staircase and exhibits helicase activities toward dual-forked DNA. Together, we reveal the supramolecular assembly of SIR2-HerA as a unique mechanism for switching enzymatic activities and bolstering anti-phage defense strategies.

PubMed: 38096827
DOI: 10.1016/j.molcel.2023.11.007

実験手法

ELECTRON MICROSCOPY (3.25 Å)