7c11

Formate--tetrahydrofolate ligase from Methylobacterium extorquens CM4 strain

spinqualitylabelsall models 7c11, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c11 is a 8 chain structure with sequence from Methylorubrum extorquens CM4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.815Å Ligands: ACT, FLC, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTHS_METC4 Publication Abstract from PubMed 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 Km 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 A 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. Biochemical properties and crystal structure of formate-tetrahydrofolate ligase from Methylobacterium extorquens CM4.,Kim S, Lee SH, Seo H, Kim KJ Biochem Biophys Res Commun. 2020 Jul 30;528(3):426-431. doi:, 10.1016/j.bbrc.2020.05.198. Epub 2020 Jun 4. PMID:32505353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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