1qzf: Difference between revisions
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'''Crystal structure of DHFR-TS from Cryptosporidium hominis''' | {{Structure | ||
|PDB= 1qzf |SIZE=350|CAPTION= <scene name='initialview01'>1qzf</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=UMP:2'-DEOXYURIDINE+5'-MONOPHOSPHATE'>UMP</scene>, <scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of DHFR-TS from Cryptosporidium hominis''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QZF is a [ | 1QZF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZF OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14555647 14555647] | ||
[[Category: Cryptosporidium hominis]] | [[Category: Cryptosporidium hominis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: bifunctional enzyme]] | [[Category: bifunctional enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:50 2008'' | ||
Revision as of 14:44, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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