Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

5,10-methylenetetrahydrofolate reductase (MTHFR) commits folate-derived one-carbon units to generate the methyl-donor s -adenosyl- l -methionine (SAM). Eukaryotic MTHFR appends to the well-conserved catalytic domain (CD) a unique regulatory domain (RD) that confers feedback inhibition by SAM. Here w...

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Bibliographic Details
Published in:	Nature communications Vol. 15; no. 1; p. 3248
Main Authors:	Blomgren, Linnea K. M., Huber, Melanie, Mackinnon, Sabrina R., Bürer, Céline, Baslé, Arnaud, Yue, Wyatt W., Froese, D. Sean, McCorvie, Thomas J.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 15-04-2024 Nature Publishing Group Nature Portfolio
Subjects:	101/28 5, 10-Methylenetetrahydrofolate reductase (FADH2) 631/45/173 631/45/607 631/535/1258/1259 631/57 82/80 Acoustic microscopes Allosteric properties Allosteric Regulation Asymmetry Binding sites Catalysis Cellular structure Conformation Cryoelectron Microscopy Crystal structure Electron microscopy Enzymatic activity Enzymes Feedback inhibition Flexibility Folic acid Homocysteine Humanities and Social Sciences Humans Inserts L-Homocysteine Methionine Methylation Methylenetetrahydrofolate reductase Methylenetetrahydrofolate Reductase (NADPH2) - chemistry Microscopy multidisciplinary Proteins Reductases Regulatory mechanisms (biology) S-Adenosylmethionine - metabolism Scanning acoustic microscopy Science Science (multidisciplinary) Signal transduction Substrates Symmetry
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