Article
Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases.
Proteins - 1 Jan 1990
Perry K M, Fauman E B, Finer-Moore J S, Montfort W R, Maley G F, Maley F, Stroud R M
Abstract excerpt
The structure of thymidylate synthase (TS) from Escherichia coli was solved from cubic crystals with a = 133 A grown under reducing conditions at pH 7.0, and refined to R = 22% at 2.1 A resolution. The structure is compared with that from Lactobacillus casei solved to R = 21% at 2.3 A resolution....
Topics
- Amino Acid Sequence
- Animals
- Computer Graphics
- Computer Simulation
- Crystallography
- Escherichia coli
- Humans
- Lacticaseibacillus casei
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Structure-Activity Relationship
- Thymidylate Synthase