Purification, crystallization, and preliminary X-ray studies of 10-formyltetrahydrofolate synthetase from Clostridia acidici-urici.
The monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and crystallized. The crystals belong to space group P2(1), with unit cell dimensions a = 102.4 A, b = 116.5 A, c = 115.8 A, and beta = 103.5. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme tetramer, and a specific volume of the unit cell of 2.7 A3/ Da. The crystals diffract to at least 2.3 A resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector.
D'Ari
L
L
Department of Molecular and Cell Biology, University of California, Berkeley, USA.
Cheung
E
E
Rabinowitz
J C
JC
Bolduc
J M
JM
Huang
J Y
JY
Stoddard
B L
BL
D001426:Bacterial Proteins / Q000737:chemistry*; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005574:Formate-Tetrahydrofolate Ligase / Q000737:chemistry*; D002955:Leucovorin / Q000031:analogs & derivatives / Q000096:biosynthesis
D001426:Bacterial Proteins; C010161:10-formyltetrahydropteroylglutamic acid; D005574:Formate-Tetrahydrofolate Ligase; D002955:Leucovorin