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2YJT

Crystal structure of E. coli DEAD-box protein SrmB bound to regulator of ribonuclease activity A (RraA)

2YJT の概要
エントリーDOI10.2210/pdb2yjt/pdb
関連するPDBエントリー2YJV
分子名称REGULATOR OF RIBONUCLEASE ACTIVITY A, ATP-DEPENDENT RNA HELICASE SRMB (3 entities in total)
機能のキーワードhydrolase inhibitor-hydrolase complex, dead box rna helicases, hydrolase inhibitor/hydrolase
由来する生物種ESCHERICHIA COLI
詳細
タンパク質・核酸の鎖数4
化学式量合計71673.32
構造登録者
Pietras, Z.,Hardwick, S.W.,Luisi, B.F. (登録日: 2011-05-23, 公開日: 2012-06-06, 最終更新日: 2023-12-20)
主引用文献Pietras, Z.,Hardwick, S.W.,Swiezewski, S.,Luisi, B.F.
Potential Regulatory Interactions of Escherichia Coli Rraa Protein with Dead-Box Helicases.
J.Biol.Chem., 288:31919-, 2013
Cited by
PubMed Abstract: Members of the DEAD-box family of RNA helicases contribute to virtually every aspect of RNA metabolism, in organisms from all domains of life. Many of these helicases are constituents of multicomponent assemblies, and their interactions with partner proteins within the complexes underpin their activities and biological function. In Escherichia coli the DEAD-box helicase RhlB is a component of the multienzyme RNA degradosome assembly, and its interaction with the core ribonuclease RNase E boosts the ATP-dependent activity of the helicase. Earlier studies have identified the regulator of ribonuclease activity A (RraA) as a potential interaction partner of both RNase E and RhlB. We present structural and biochemical evidence showing how RraA can bind to, and modulate the activity of RhlB and another E. coli DEAD-box enzyme, SrmB. Crystallographic structures are presented of RraA in complex with a portion of the natively unstructured C-terminal tail of RhlB at 2.8-Å resolution, and in complex with the C-terminal RecA-like domain of SrmB at 2.9 Å. The models suggest two distinct mechanisms by which RraA might modulate the activity of these and potentially other helicases.
PubMed: 24045937
DOI: 10.1074/JBC.M113.502146
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 2yjt
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2026-04-29に公開中

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