2BW0

Crystal Structure of the hydrolase domain of Human 10-Formyltetrahydrofolate 2 dehydrogenase

Summary for 2BW0

• Entry DOI: 10.2210/pdb2bw0/pdb
• Descriptor: 10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE, SULFATE ION (3 entities in total)
• Functional Keywords: dehydrogenase, nucleotide biosynthesis, oxidoreductase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: O75891
• Total number of polymer chains: 1
• Total formula weight: 36671.68

Authors

Ogg, D.J.,Stenmark, P.,Arrowsmith, C.,Edwards, A.,Ehn, M.,Graslund, S.,Hammarstrom, M.,Hallberg, M.,Kotenyova, T.,Nilsson-Ehle, P.,Nordlund, P.,Persson, C.,Sagemark, J.,Schuler, H.,Sundstrom, M.,Thorsell, A.,Dobritzsch, D.,Weigelt, J. (deposition date: 2005-07-07, release date: 2005-07-08, Last modification date: 2023-12-13)

Primary citation

Kursula, P.,Schuler, H.,Flodin, S.,Nilsson-Ehle, P.,Ogg, D.J.,Savitsky, P.,Nordlund, P.,Stenmark, P.
Structures of the Hydrolase Domain of Human 10-Formyltetrahydrofolate Dehydrogenase and its Complex with a Substrate Analogue.
Acta Crystallogr.,Sect.D, 62:1294-, 2006

PubMed Abstract: 10-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.

PubMed: 17057331
DOI: 10.1107/S0907444906026849

Experimental method

X-RAY DIFFRACTION (1.7 Å)