Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase.
1992; National Academy of Sciences; Volume: 89; Issue: 13 Linguagem: Inglês
10.1073/pnas.89.13.6114
ISSN1091-6490
AutoresRobert J. Almassy, Cheryl A. Janson, C. Kan, Zuzana Hostomska,
Tópico(s)Enzyme Structure and Function
ResumoThe three-dimensional structure of phosphoribosylglycinamide formyltransferase (10-formyltetrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2) has been solved both as an apoenzyme at 2.8-A resolution and as a ternary complex with the substrate glycinamide ribonucleotide and a folate inhibitor at 2.5-A resolution. The structure is a modified doubly wound alpha/beta sheet with flexibility in the active site, including a disordered loop in the apo structure, which is ordered in the ternary complex structure. This enzyme is a target for anti-cancer therapy and now for structure-based drug design.
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