Crystal structure of the thymidylate synthase R166Q mutant

Crystal structures of thymidylate synthase mutant R166Q: Structural basis for the nearly complete loss of catalytic activity.

Crystallographics studied of thymidylate synthase: structure of a mammalian enzyme and analyses of invariant non-catalytic residues in a bacterial enzyme

(CXM)KQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLQGDTNIAYLHENN
VTIWDEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVAD
GKLSCQLYQQSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKP
ESIFDYRFEDFEIEGYDPHPGIKAPVAI

MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLQGDTNIAYLHENNVTIW
DEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLS
CQLYQQSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIF
DYRFEDFEIEGYDPHPGIKAPVAI

Ammonium sulfate, potassium sulfate, EDTA, DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

1FFL contains the same protein in the absence of ligands (apo-TS)

The biological assembly is a dimer constructed from chains A and B. Both dimers are contained in the assymetric unit in this space group

MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLQGDTNIAYLHENNVTIW
DEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLS
CQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIF
DYRFEDFEIEGYDPHPGIKAPVAI