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EC Number	Crystallization (Commentary)
1.4.1.27	component T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, mimicking the ternary complex in the reverse reaction. The complex shows a highly interacting intermolecular interface limited to a small area and the protein-bound dihydrolipoyllysine arm inserted into the active site cavity of the T-protein. Invariant residue Arg292 of the T-protein is essential for complex assembly
1.4.1.27	structure of component T-protein, at 1.5 A resolution. The dimeric state might be essential for the function. The role of residue Glu100 might be the activation of the N10 atom of tetrahodrofolate by increasing its nucleophilic character. The H-protein-T-protein interface includes invariant residues Arg327, Tyr330, and Arg376 of domain III, and Lys20, Phe24, Gly26, Ser35, Ile36, Leu248, Gly249, Asp252, Thr253, Arg255, and Leu262 of domains I and II
1.4.1.27	structures of component T-protein in the apoform, the tetrahydrofolate complex, the folinic acid complex, and the lipoic acid complex. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding

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Release 2023.1 (January 2023)