1b0a
From Proteopedia
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5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI.
Overview
The structure of a bifunctional 5,10-methylene-tetrahydrofolate, dehydrogenase/cyclohydrolase from Escherichia coli has been determined at, 2.5 A resolution in the absence of bound substrates and compared to the, NADP-bound structure of the homologous enzyme domains from a trifunctional, human synthetase enzyme. Superposition of these structures allows the, identification of a highly conserved cluster of basic residues that are, appropriately positioned to serve as a binding site for the, poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling, studies and molecular dynamic simulations of bound, methylene-tetrahydrofolate and NADP shows that this binding site would, allow interaction of the nicotinamide and pterin rings in the, dehydrogenase active site. Comparison of these enzymes also indicates, differences between their active sites that might allow the development of, inhibitors specific to the bacterial target.
About this Structure
1B0A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase., Shen BW, Dyer DH, Huang JY, D'Ari L, Rabinowitz J, Stoddard BL, Protein Sci. 1999 Jun;8(6):1342-9. PMID:10386884
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