4U2H

The crystal structure of apo CalE6, a methionine gamma lyase from Micromonospora echinospora

4U2H の概要

• エントリーDOI: 10.2210/pdb4u2h/pdb
• 関連するPDBエントリー: 4U1T
• 分子名称: CalE6, SULFATE ION (3 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Micromonospora echinospora
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 335562.76

構造登録者

Song, H.G.,Xu, R. (登録日: 2014-07-17, 公開日: 2015-01-07, 最終更新日: 2024-03-20)

主引用文献

Song, H.,Xu, R.,Guo, Z.
Identification and Characterization of a Methionine gamma-Lyase in the Calicheamicin Biosynthetic Cluster of Micromonospora echinospora
Chembiochem, 16:100-109, 2015

PubMed Abstract: CalE6 is a previously uncharacterized protein involved in the biosynthesis of calicheamicins in Micromonospora echinospora. It is a pyridoxal-5'-phosphate-dependent enzyme and exhibits high sequence homology to cystathionine γ-lyases and cystathionine γ-synthases. However, it was found to be active towards methionine and to convert this amino acid into α-ketobutyrate, ammonium, and methanethiol. The crystal structure of the cofactor-bound holoenzyme was resolved at 2.0 Å; it contains two active site residues, Gly105 and Val322, specific for methionine γ-lyases. Modeling of methionine into the active site allows identification of the active site residues responsible for substrate recognition and catalysis. These findings support that CalE6 is a putative methionine γ-lyase producing methanethiol as a building block in biosynthesis of calicheamicins.

PubMed: 25404066
DOI: 10.1002/cbic.201402489

実験手法

X-RAY DIFFRACTION (1.85 Å)