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. 1992 Jul 1;89(13):6114–6118. doi: 10.1073/pnas.89.13.6114

Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase.

R J Almassy 1, C A Janson 1, C C Kan 1, Z Hostomska 1
PMCID: PMC49448  PMID: 1631098

Abstract

The 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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Selected References

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