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3AIA

Crystal structure of DUF358 reveals a putative SPOUT-class methltransferase

3AIA の概要
エントリーDOI10.2210/pdb3aia/pdb
関連するPDBエントリー3AI9
分子名称UPF0217 protein MJ1640, S-ADENOSYLMETHIONINE, pentane-2,2,4,4-tetrol, ... (4 entities in total)
機能のキーワードduf358, rrna methyltransferase, spout-class fold, transferase
由来する生物種Methanocaldococcus jannaschii (Methanococcus jannaschii)
タンパク質・核酸の鎖数2
化学式量合計49693.20
構造登録者
Yuan, Y.A.,Chen, H.Y. (登録日: 2010-05-11, 公開日: 2011-03-30, 最終更新日: 2023-11-01)
主引用文献Chen, H.Y.,Yuan, Y.A.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase
J Mol Cell Biol, 2:366-374, 2010
Cited by
PubMed Abstract: The proteins in DUF358 family are all bacterial proteins, which are ∼200 amino acids long with unknown function. Bioinformatics analysis suggests that these proteins contain several conserved arginines and aspartates that might adopt SPOUT-class fold. Here we report crystal structure of Methanocaldococcus jannaschii DUF358/Mj1640 in complex with S-adenosyl-L-methionine (SAM) at 1.4 Å resolution. The structure reveals a single domain structure consisting of eight-stranded β-sheets sandwiched by six α-helices at both sides. Similar to other SPOUT-class members, Mj1640 contains a typical deep trefoil knot at its C-terminus to accommodate the SAM cofactor. However, Mj1640 has limited structural extension at its N-terminus, which is unique to this family member. Mj1640 forms a dimer, which is mediated by two parallel pairs of α-helices oriented almost perpendicular to each other. Although Mj1640 shares close structural similarity with Nep1, the significant differences in N-terminal extension domain and the overall surface charge distribution strongly suggest that Mj1640 might target a different RNA sequence. Detailed structural analysis of the SAM-binding pocket reveals that Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation.
PubMed: 21098051
DOI: 10.1093/jmcb/mjq034
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 3aia
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2025-12-31に公開中

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