4CNF

Crystal structure of Sulfolobus acidocaldarius TrmJ

4CNF の概要

• エントリーDOI: 10.2210/pdb4cnf/pdb
• 関連するPDBエントリー: 4CND 4CNE 4CNG
• 分子名称: SPOU RRNA METHYLASE, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: transferase, trna 2'-o-methyltransferase, spout
• 由来する生物種: SULFOLOBUS ACIDOCALDARIUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58749.49

構造登録者

Van Laer, B.,Somme, J.,Roovers, M.,Steyaert, J.,Droogmans, L.,Versees, W. (登録日: 2014-01-22, 公開日: 2014-07-02, 最終更新日: 2023-12-20)

主引用文献

Somme, J.,Van Laer, B.,Roovers, M.,Steyaert, J.,Versees, W.,Droogmans, L.
Characterization of Two Homologous 2'-O-Methyltransferases Showing Different Specificities for Their tRNA Substrates.
RNA, 20:1257-, 2014

PubMed Abstract: The 2'-O-methylation of the nucleoside at position 32 of tRNA is found in organisms belonging to the three domains of life. Unrelated enzymes catalyzing this modification in Bacteria (TrmJ) and Eukarya (Trm7) have already been identified, but until now, no information is available for the archaeal enzyme. In this work we have identified the methyltransferase of the archaeon Sulfolobus acidocaldarius responsible for the 2'-O-methylation at position 32. This enzyme is a homolog of the bacterial TrmJ. Remarkably, both enzymes have different specificities for the nature of the nucleoside at position 32. While the four canonical nucleosides are substrates of the Escherichia coli enzyme, the archaeal TrmJ can only methylate the ribose of a cytidine. Moreover, the two enzymes recognize their tRNA substrates in a different way. We have solved the crystal structure of the catalytic domain of both enzymes to gain better understanding of these differences at a molecular level.

PubMed: 24951554
DOI: 10.1261/RNA.044503.114

実験手法

X-RAY DIFFRACTION (1.4 Å)