PMID:9061797
| Citation |
Cheung, E, D'Ari, L, Rabinowitz, JC, Dyer, DH, Huang, JY and Stoddard, BL (1997) Purification, crystallization, and preliminary x-ray studies of a bifunctional 5,10-methenyl/methylene-tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli. Proteins 27:322-4 |
|---|---|
| Abstract |
A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10-methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals belong to space group I222, with unit cell dimensions of a = 64.5 A, b = 84.9 A, c = 146.1 A. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme monomer, and a specific volume of the unit cell of 3.2 A3/Da. The crystals diffract to at least 2.8 A resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector. A 2.56 A resolution native data set has been collected at beamline X12-C at the NSLS. |
| Links | |
| Keywords |
Aminohydrolases/chemistry; Aminohydrolases/isolation & purification; Bacterial Proteins/chemistry; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli/enzymology; Methylenetetrahydrofolate Dehydrogenase (NADP)/chemistry; Methylenetetrahydrofolate Dehydrogenase (NADP)/isolation & purification; Multienzyme Complexes/chemistry; Multienzyme Complexes/isolation & purification |
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