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Crystal Structure of the hydrolase domain of Human 10-Formyltetrahydrofolate 2 dehydrogenaseCrystal Structure of the hydrolase domain of Human 10-Formyltetrahydrofolate 2 dehydrogenase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed10-Formyltetrahydrofolate dehydrogenase is a ubiquitously expressed enzyme in the human body. It catalyses the formation of tetrahydrofolate and carbon dioxide from 10-formyltetrahydrofolate, thereby playing an important role in the human metabolism of one-carbon units. It is a two-domain protein in which the N-terminal domain hydrolyses 10-formyltetrahydrofolate into formate and tetrahydrofolate. The high-resolution crystal structure of the hydrolase domain from human 10-formyltetrahydrofolate dehydrogenase has been determined in the presence and absence of a substrate analogue. The structures reveal conformational changes of two loops upon ligand binding, while key active-site residues appear to be pre-organized for catalysis prior to substrate binding. Two water molecules in the structures mark the positions of key oxygen moieties in the catalytic reaction and reaction geometries are proposed based on the structural data. Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue.,Kursula P, Schuler H, Flodin S, Nilsson-Ehle P, Ogg DJ, Savitsky P, Nordlund P, Stenmark P Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1294-9. Epub 2006, Oct 18. PMID:17057331[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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