2FCA

The structure of BsTrmB

2FCA の概要

• エントリーDOI: 10.2210/pdb2fca/pdb
• 分子名称: tRNA (guanine-N(7)-)-methyltransferase, POTASSIUM ION (3 entities in total)
• 機能のキーワード: methyltransferase, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49423.04

構造登録者

Zegers, I.,Van Vliet, F.,Bujnicki, J.,Kosinski, J.,Gigot, D.,Droogmans, L. (登録日: 2005-12-12, 公開日: 2006-08-15, 最終更新日: 2024-02-14)

主引用文献

Zegers, I.,Gigot, D.,van Vliet, F.,Tricot, C.,Aymerich, S.,Bujnicki, J.M.,Kosinski, J.,Droogmans, L.
Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase.
Nucleic Acids Res., 34:1925-1934, 2006

PubMed Abstract: The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 A. This is the first structure of a member of the TrmB family to be determined by X-ray crystallography. It reveals a unique variant of the Rossmann-fold methyltransferase (RFM) structure, with the N-terminal helix folded on the opposite site of the catalytic domain. The architecture of the active site and a computational docking model of BsTrmB in complex with the methyl group donor S-adenosyl-L-methionine and the tRNA substrate provide an explanation for results from mutagenesis studies of an orthologous enzyme from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown here to be dimeric both in the crystal and in solution. The dimer interface has a hydrophobic core and buries a potassium ion and five water molecules. The evolutionary analysis of the putative interface residues in the TrmB family suggests that homodimerization may be a specific feature of TrmBs from Bacilli, which may represent an early stage of evolution to an obligatory dimer.

PubMed: 16600901
DOI: 10.1093/nar/gkl116

実験手法

X-RAY DIFFRACTION (2.1 Å)