Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.6
Classification:TRANSFERASE
Release Date:2006-05-02
Deposition Date:2006-01-24
Revision Date:2008-05-01#2011-07-13
Molecular Weight:31312.17
Macromolecule Type:Protein
Residue Count:264
Atom Site Count:2253
DOI:10.2210/pdb2ftn/pdb
Abstract:
Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
Resolution:1.6
Classification:TRANSFERASE
Release Date:2006-05-02
Deposition Date:2006-01-24
Revision Date:2008-05-01#2011-07-13
Molecular Weight:31312.17
Macromolecule Type:Protein
Residue Count:264
Atom Site Count:2253
DOI:10.2210/pdb2ftn/pdb
Abstract:
Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
| Date made available | 2006 |
|---|---|
| Publisher | RCSB-PDB |