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| {{STRUCTURE_1qzf| PDB=1qzf | SCENE= }} | | {{STRUCTURE_1qzf| PDB=1qzf | SCENE= }} |
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| '''Crystal structure of DHFR-TS from Cryptosporidium hominis'''
| | ===Crystal structure of DHFR-TS from Cryptosporidium hominis=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14555647}}, adds the Publication Abstract to the page |
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| | {{ABSTRACT_PUBMED_14555647}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stroud, R M.]] | | [[Category: Stroud, R M.]] |
| [[Category: Bifunctional enzyme]] | | [[Category: Bifunctional enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:53:37 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:15:38 2008'' |
