3GQU
Pyrococcus Horikoshii NOP5 RNA Binding Domain
3GQU の概要
| エントリーDOI | 10.2210/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 | |
| 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: 19336398DOI: 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) |
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