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3GQU

Pyrococcus Horikoshii NOP5 RNA Binding Domain

3GQU の概要
エントリーDOI10.2210/pdb3gqu/pdb
関連するPDBエントリー3GQX
分子名称NOP5P PROTEIN, IODIDE ION (3 entities in total)
機能のキーワードrna binding domain, rna binding protein
由来する生物種Pyrococcus horikoshii
詳細
タンパク質・核酸の鎖数1
化学式量合計20504.12
構造登録者
Reyes, F.E.,Hardin, J.W.,Batey, R.T. (登録日: 2009-03-24, 公開日: 2009-04-21, 最終更新日: 2024-02-21)
主引用文献Hardin, J.W.,Reyes, F.E.,Batey, R.T.
Analysis of a Critical Interaction within the Archaeal Box C/D Small Ribonucleoprotein Complex
J.Biol.Chem., 284:15317-15324, 2009
Cited by
PubMed Abstract: In archaea and eukarya, box C/D ribonucleoprotein (RNP) complexes are responsible for 2'-O-methylation of tRNAs and rRNAs. The archaeal box C/D small RNP complex requires a small RNA component (sRNA) possessing Watson-Crick complementarity to the target RNA along with three proteins: L7Ae, Nop5p, and fibrillarin. Transfer of a methyl group from S-adenosylmethionine to the target RNA is performed by fibrillarin, which by itself has no affinity for the sRNA-target duplex. Instead, it is targeted to the site of methylation through association with Nop5p, which in turn binds to the L7Ae-sRNA complex. To understand how Nop5p serves as a bridge between the targeting and catalytic functions of the box C/D small RNP complex, we have employed alanine scanning to evaluate the interaction between the Pyrococcus horikoshii Nop5p domain and an L7Ae box C/D RNA complex. From these data, we were able to construct an isolated RNA-binding domain (Nop-RBD) that folds correctly as demonstrated by x-ray crystallography and binds to the L7Ae box C/D RNA complex with near wild type affinity. These data demonstrate that the Nop-RBD is an autonomously folding and functional module important for protein assembly in a number of complexes centered on the L7Ae-kinkturn RNP.
PubMed: 19336398
DOI: 10.1074/jbc.M901368200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 3gqu
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2026-04-22に公開中

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