1qzf
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Crystal structure of DHFR-TS from Cryptosporidium hominis
OverviewOverview
We have determined the crystal structure of dihydrofolate, reductase-thymidylate synthase (DHFR-TS) from Cryptosporidium hominis, revealing a unique linker domain containing an 11-residue alpha-helix that, has extensive interactions with the opposite DHFR-TS monomer of the, homodimeric enzyme. Analysis of the structure of DHFR-TS from C. hominis, and of previously solved structures of DHFR-TS from Plasmodium falciparum, and Leishmania major reveals that the linker domain primarily controls the, relative orientation of the DHFR and TS domains. Using the tertiary, structure of the linker domains, we have been able to place a number of, protozoa in two distinct and dissimilar structural families corresponding, to two evolutionary families and provide the first structural evidence, validating the use of DHFR-TS as a tool of phylogenetic classification., Furthermore, the structure of C. hominis DHFR-TS calls into question, surface electrostatic channeling as the universal means of dihydrofolate, transport between TS and DHFR in the bifunctional enzyme.
About this StructureAbout this Structure
1QZF is a Single protein structure of sequence from Cryptosporidium hominis with UMP, CB3, FOL and NDP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase., O'Neil RH, Lilien RH, Donald BR, Stroud RM, Anderson AC, J Biol Chem. 2003 Dec 26;278(52):52980-7. Epub 2003 Oct 9. PMID:14555647
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