6J4C

Crystal structure of MarH, an epimerase for biosynthesis of Maremycins in Streptomyces, under 10 mM ZnSO4

6J4C の概要

• エントリーDOI: 10.2210/pdb6j4c/pdb
• 関連するPDBエントリー: 6J4B 6J4D
• 分子名称: Cupin superfamily protein, ZINC ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: isomerase, epimerase, maremycins, biosynthesis
• 由来する生物種: Streptomyces sp. B9173
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13671.66

構造登録者

Hou, Y.,Liu, B.,Hu, K.,Zhang, R. (登録日: 2019-01-08, 公開日: 2020-01-15, 最終更新日: 2024-03-27)

主引用文献

Liu, B.,Hou, Y.,Wang, X.,Ma, X.,Fang, S.,Huang, T.,Chen, Y.,Bai, Z.,Lin, S.,Zhang, R.,Hu, K.
Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH.
Org.Biomol.Chem., 17:9605-9614, 2019

PubMed Abstract: Diverse derivatives of amino acids with different steric configurations are important biosynthetic building blocks. In biology, epimerization is an important way to generate steric diversity. MarH catalyzes the epimerization of the β-position of (3R)-β-methyl-indolepyruvate (MeInPy), forming (3S)-β-MeInPy. Both compounds are derivatives of l-tryptophan (l-Trp) and are important precursors of bioactive natural products. Here, we report the crystal structures of MarH and the NMR structure of its complex with l-Trp, an analogue of its native substrate, (3R)-β-MeInPy. Structural analysis and mutagenesis studies indicated that His25 acts as a base to remove H and generate a planar carbanion intermediate, which is then putatively reprotonated on the opposite face by a water molecule to form (3S)-β-MeInPy in a stereospecific manner. The details of β-site isomerization at the atomic level provide deeper insights into the epimerization mechanism of MarH and will facilitate further enzyme design to extend the substrate scope.

PubMed: 31681917
DOI: 10.1039/c9ob01996k

実験手法

X-RAY DIFFRACTION (1.58 Å)