7C11

Formate--tetrahydrofolate ligase from Methylobacterium extorquens CM4 strain

7C11 の概要

• エントリーDOI: 10.2210/pdb7c11/pdb
• 分子名称: Formate-tetrahydrofolate ligase, L(+)-TARTARIC ACID, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: formate assimilation, methylobacterium extorquens cm4, formate-tetrahydrofolate ligase, metal usage, ligase
• 由来する生物種: Methylorubrum extorquens (strain CM4 / NCIMB 13688)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 487124.36

構造登録者

Kim, K.-J.,Kim, S.,Seo, H.,Lee, S. (登録日: 2020-05-02, 公開日: 2020-10-28, 最終更新日: 2023-11-29)

主引用文献

Kim, S.,Lee, S.H.,Seo, H.,Kim, K.J.
Biochemical properties and crystal structure of formate-tetrahydrofolate ligase from Methylobacterium extorquens CM4.
Biochem.Biophys.Res.Commun., 528:426-431, 2020

PubMed Abstract: Methylobacterium extorquens is a methylotroph model organism that has the ability to assimilate formate using the tetrahydrofolate (THF) pathway. The formate-tetrahydrofolate ligase from M. extorquens (MeFtfL) is an enzyme involved in the THF pathway that catalyzes the conversion of formate, THF, and ATP into formyltetrahydrofolate and ADP. To investigate the biochemical properties of MeFtfL, we evaluated the metal usage and enzyme kinetics of the enzyme. MeFtfL uses the Mg ion for catalytic activity, but also has activity for Mn and Ca ions. The enzyme kinetics analysis revealed that K value of farmate was much higher than THF and ATP, which shows that the ligation activity of MeFtfL is highly dependent on formation concentration. We also determined the crystal structure of MeFtfL at 2.8 Å resolution. MeFtfL functions as a tetramer, and each monomer consists of three domains. The structural superposition of MeFtfL with FtfL from Moorella thermoacetica allowed us to predict the substrate binding site of the enzyme.

PubMed: 32505353
DOI: 10.1016/j.bbrc.2020.05.198

実験手法

X-RAY DIFFRACTION (2.815 Å)