Article
Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Biochemistry - 23 Apr 1996
Finer-Moore J S, Liu L, Schafmeister C E, Birdsall D L, Mau T, Santi D V, Stroud R M
Abstract excerpt
Thymidylate synthase (TS) methylates only dUMP, not dCMP. The crystal structure of TS.dCMP shows sCMP 4-NH2 excluded from the space between Asn-229 and His-199 by the hydrogen bonding and steric properties and Asn-229. Consequently, 6-C of dCMP is over 4 A from the active site sulfhydryl. The Asn...
Topics
- Asparagine
- Binding Sites
- Crystallography, X-Ray
- Cysteine
- Deoxycytidine Monophosphate
- Deoxyuracil Nucleotides
- Hydrogen Bonding
- Kinetics
- Methylation
- Models, Molecular
- Molecular Conformation
- Molecular Sequence Data
- Mutation
- Recombinant Proteins
- Substrate Specificity