Literature summary extracted from

Dams, T.; Auerbach, G.; Bader, G.; Jacob, U.; Ploom, T.; Huber, R.; Jaenicke, R.
The crystal structure of dihydrofolate reductase from Thermotoga maritima Molecular features of thermostability (2000), J. Mol. Biol., 297, 659-672 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.5.1.3	expression in Escherichia coli	Thermotoga maritima

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.5.1.3	vapour diffusion technique at 18°C, two high-resolution structures of dihydrofolate reductase in its unliganded state, and in its ternary complex with the cofactor NADPH and the inhibitor, methotrexate	Thermotoga maritima

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.5.1.3	methotrexate	-	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.5.1.3	Thermotoga maritima	Q60034	-	-
1.5.1.3	Thermotoga maritima DSM 3109	Q60034	-	-

Subunits

EC Number	Subunits	Comment	Organism
1.5.1.3	homodimer	-	Thermotoga maritima

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.5.1.3	additional information	-	molecular reasons for the high intrinsic stability of the enzyme: the molecule is extremely rigid, even with respect to structural changes during substrate binding and turnover. Major contributions to the high intrinsic stability of the enzyme result from the formation of the dimer. Within the monomer, only subtle stabilizing interactions are detectable. The docking of the subunits is optimized with respect to high packing density in the dimer interface, additional salt-bridges and beta-sheets	Thermotoga maritima

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Release 2023.1 (January 2023)