7PZZ

Crystal structure of serine hydroxymethyltransferase, isoform 2 from Arabidopsis thaliana (SHM2)

7PZZ の概要

• エントリーDOI: 10.2210/pdb7pzz/pdb
• 関連するPDBエントリー: 7Q00 7QPE 7QX8
• 分子名称: Serine hydroxymethyltransferase 2, mitochondrial, 1,2-ETHANEDIOL, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: c1 metabolism, tetrahydrofolate, tetramer, plp-dependent enzyme, mitochondria, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 217711.07

構造登録者

Ruszkowski, M.,Sekula, B. (登録日: 2021-10-13, 公開日: 2022-08-24, 最終更新日: 2024-01-31)

主引用文献

Nogues, I.,Sekula, B.,Angelaccio, S.,Grzechowiak, M.,Tramonti, A.,Contestabile, R.,Ruszkowski, M.
Arabidopsis thaliana serine hydroxymethyltransferases: functions, structures, and perspectives.
Plant Physiol Biochem., 187:37-49, 2022

PubMed Abstract: Serine hydroxymethyltransferase (SHM) is one of the hallmarks of one-carbon metabolism. In plants, isoforms of SHM participate in photorespiration and/or transfer the one-carbon unit from L-serine to tetrahydrofolate (THF), hence producing 5,10-CH-THF that is needed, e.g., for biosynthesis of methionine, thymidylate, and purines. These links highlight the importance of SHM activity in DNA biogenesis, its epigenetic methylations, and in stress responses. Plant genomes encode several SHM isoforms that localize to cytosol, mitochondria, plastids, and nucleus. In this work, we present a thorough functional and structural characterization of all seven SHM isoforms from Arabidopsis thaliana (AtSHM1-7). In particular, we analyzed tissue-specific expression profiles of the AtSHM genes. We also compared catalytic properties of the active AtSHM1-4 in terms of catalytic efficiency in both directions and inhibition by the THF substrate. Despite numerous attempts to rescue the SHM activity of AtSHM5-7, we failed, which points towards different physiological functions of these isoforms. Comparative analysis of experimental and predicted three-dimensional structures of AtSHM1-7 proteins indicated differences in regions that surround the entrance to the active site cavity.

PubMed: 35947902
DOI: 10.1016/j.plaphy.2022.07.025

実験手法

X-RAY DIFFRACTION (1.65 Å)