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5FT1

Crystal structure of gp37(Dip) from bacteriophage phiKZ bound to RNase E of Pseudomonas aeruginosa

5FT1 の概要
エントリーDOI10.2210/pdb5ft1/pdb
関連するPDBエントリー5FT0
分子名称GP37, RIBONUCLEASE E (3 entities in total)
機能のキーワードhydrolase-inhibitor complex, dip, phikz, bacteriophage, rnase e, ribonuclease inhibitor, rna degradosome, pseudomonas aeruginosa, hydrolase/inhibitor
由来する生物種PSEUDOMONAS PHAGE PHIKZ
詳細
細胞内の位置Cytoplasm : Q9HZM8
タンパク質・核酸の鎖数12
化学式量合計208172.16
構造登録者
主引用文献Van den Bossche, A.,Hardwick, S.W.,Ceyssens, P.J.,Hendrix, H.,Voet, M.,Dendooven, T.,Bandyra, K.J.,De Maeyer, M.,Aertsen, A.,Noben, J.P.,Luisi, B.F.,Lavigne, R.
Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome.
Elife, 5:-, 2016
Cited by
PubMed Abstract: In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection. We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host. Encoded by giant phage фKZ, this protein associates with two RNA binding sites of the RNase E component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resulting in effective inhibition of RNA degradation and processing. The 2.2 Å crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues. Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E. Through the activity of Dip, фKZ has evolved a unique mechanism to down regulate a key metabolic process of its host to allow accumulation of viral RNA in infected cells.
PubMed: 27447594
DOI: 10.7554/eLife.16413
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.75 Å)
構造検証レポート
Validation report summary of 5ft1
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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