3NGL

Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from Thermoplasma acidophilum

Summary for 3NGL

• Entry DOI: 10.2210/pdb3ngl/pdb
• Related: 3NGX
• Descriptor: Bifunctional protein folD, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: methylenetetrahydrofolate dehydrogenase/cyclohydrolase, catalyzes the oxidation of 5, 10-methylenetetrahydrofolate to 5, 10-methenyltetrahydrofolate, the hydrolysis of 5, 10-methenyltetrahydrofolate to 10-formyltetrahydrofolate, oxidoreductase, hydrolase
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 2
• Total formula weight: 62805.37

Authors

Sung, M.W.,Lee, W.H.,Hwang, K.Y. (deposition date: 2010-06-12, release date: 2011-04-20, Last modification date: 2024-03-20)

Primary citation

Lee, W.H.,Sung, M.W.,Kim, J.H.,Kim, Y.K.,Han, A.,Hwang, K.Y.
Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum
Biochem.Biophys.Res.Commun., 406:459-463, 2011

PubMed Abstract: Folate co-enzymes play a pivotal role in one-carbon transfer cellular processes. Many eukaryotes encode the tri-functional tetrahydrofolate dehydrogenase/cyclohydrolase/synthetase (deh/cyc/syn) enzyme, which consists of a N-terminal bifunctional domain (deh/cyc) and a C-terminal monofunctional domain (syn). Here, we report the first analogous archeal enzyme structures, for the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum (TaMTHFDC) as the native protein and also as its NADP complex. The TaMTHFDC structure is a dimer with a polar interface, as well as a NADP binding site that shows minor conformational change. The orientations of the residues in the NADP binding site do not change on ligand binding, incorporating three water molecules which are hydrogen bonded with phosphate groups of NADP in the structure of the complex. Our structural information will contribute to an improved understanding of the basis of THF and one-carbon metabolism.

PubMed: 21333632
DOI: 10.1016/j.bbrc.2011.02.074

Experimental method

X-RAY DIFFRACTION (2.4 Å)