Article
Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Structure (London, England : 1993) - 15 Jul 1995
Borchert T V, Kishan K V, Zeelen J P, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga R K
Abstract excerpt
BACKGROUND: Wild-type triosephosphate isomerase (TIM) is a very stable dimeric enzyme. This dimer can be converted into a stable monomeric protein (monoTIM) by replacing the 15-residue interface loop (loop-3) by a shorter, 8-residue, loop. The crystal structure of monoTIM shows that two active-si...
Topics
- Amino Acid Sequence
- Cloning, Molecular
- Crystallography, X-Ray
- Escherichia coli
- Genetic Variation
- Histidine
- Macromolecular Substances
- Models, Molecular
- Molecular Sequence Data
- Point Mutation
- Protein Structure, Secondary
- Triose-Phosphate Isomerase