4POO

The crystal structure of Bacillus subtilis YtqB in complex with SAM

4POO の概要

• エントリーDOI: 10.2210/pdb4poo/pdb
• 関連するPDBエントリー: 4PON
• 分子名称: Putative RNA methylase, S-ADENOSYLMETHIONINE (3 entities in total)
• 機能のキーワード: rossmann-like fold, a putative methyltransferase, s-adenosyl-l-methionine, transferase
• 由来する生物種: Bacillus subtilis subsp. spizizenii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44376.53

構造登録者

Park, S.C.,Song, W.S.,Yoon, S.I. (登録日: 2014-02-26, 公開日: 2014-04-02, 最終更新日: 2023-11-08)

主引用文献

Park, S.C.,Song, W.S.,Yoon, S.I.
Structural analysis of a putative SAM-dependent methyltransferase, YtqB, from Bacillus subtilis
Biochem.Biophys.Res.Commun., 446:921-926, 2014

PubMed Abstract: S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTases) methylate diverse biological molecules using a SAM cofactor. The ytqB gene of Bacillus subtilis encodes a putative MTase and its biological function has never been characterized. To reveal the structural features and the cofactor binding mode of YtqB, we have determined the crystal structures of YtqB alone and in complex with its cofactor, SAM, at 1.9 Å and 2.2 Å resolutions, respectively. YtqB folds into a β-sheet sandwiched by two α-helical layers, and assembles into a dimeric form. Each YtqB monomer contains one SAM binding site, which shapes SAM into a slightly curved conformation and exposes the reactive methyl group of SAM potentially to a substrate. Our comparative structural analysis of YtqB and its homologues indicates that YtqB is a SAM-dependent class I MTase, and provides insights into the substrate binding site of YtqB.

PubMed: 24637210
DOI: 10.1016/j.bbrc.2014.03.026

実験手法

X-RAY DIFFRACTION (2.2 Å)