8SUW の概要
エントリーDOI | 10.2210/pdb8suw/pdb |
EMDBエントリー | 40762 40763 40778 40779 |
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, immune system |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 16 |
化学式量合計 | 843606.25 |
構造登録者 | |
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 Cited by 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: 38096827DOI: 10.1016/j.molcel.2023.11.007 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.15 Å) |
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