title: The crystal structure of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveals a novel architecture for the bifunctional enzyme.
authors.affiliation: Department of Chemistry, Dartmouth College, Burke Laboratories, Hanover, NH 03755, USA.
authors.forename: Robert H
authors.initials: RH
authors.lastname: O'Neil
authors.forename: Ryan H
authors.initials: RH
authors.lastname: Lilien
authors.forename: Bruce R
authors.initials: BR
authors.lastname: Donald
authors.forename: Robert M
authors.initials: RM
authors.lastname: Stroud
authors.forename: Amy C
authors.initials: AC
authors.lastname: Anderson
mesh_terms: D000818:Animals; D002460:Cell Line; D003458:Cryptosporidium / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry*; D011487:Protein Conformation; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry*; D013940:Thymidylate Synthase / Q000737:chemistry*
chemical_list: D009097:Multienzyme Complexes; C056930:thymidylate synthase-dihydrofolate reductase; D013762:Tetrahydrofolate Dehydrogenase; D013940:Thymidylate Synthase