2FMT

METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET

2FMT の概要

• エントリーDOI: 10.2210/pdb2fmt/pdb
• 分子名称: FORMYL-METHIONYL-TRNAFMET2, METHIONYL-TRNA FMET FORMYLTRANSFERASE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: complex (methyltransferase-trna), formyltransferase, initiation of translation, complex (methyltransferase-trna) complex, complex (methyltransferase/trna)
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118211.22

構造登録者

Schmitt, E.,Mechulam, Y.,Blanquet, S. (登録日: 1998-07-29, 公開日: 1999-07-29, 最終更新日: 2023-08-02)

主引用文献

Schmitt, E.,Panvert, M.,Blanquet, S.,Mechulam, Y.
Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
EMBO J., 17:6819-6826, 1998

PubMed Abstract: The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.

PubMed: 9843487
DOI: 10.1093/emboj/17.23.6819

実験手法

X-RAY DIFFRACTION (2.8 Å)