1trg: Difference between revisions
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E. COLI THYMIDYLATE SYNTHASE IN SYMMETRIC COMPLEX WITH CB3717 AND 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP)
OverviewOverview
BACKGROUND: Enzymes have evolved to recognise their target substrates with, exquisite selectivity and specificity. Whether fragments of the, substrate--perhaps never available to the evolving enzyme--are bound in, the same manner as the parent substrate addresses the fundamental basis of, specificity. An understanding of the relative contributions of individual, portions of ligand molecules to the enzyme-binding interaction may offer, considerable insight into the principles of substrate recognition., RESULTS: We report 12 crystal structures of Escherichia coli thymidylate, synthase in complexes with available fragments of the substrate (dUMP), both with and without the presence of a cofactor analogue. The structures, display considerable fidelity of binding mode and interactions. These, ... [(full description)]
About this StructureAbout this Structure
1TRG is a [Single protein] structure of sequence from [Escherichia coli] with UMP and CB3 as [ligands]. Active as [Thymidylate synthase], with EC number [2.1.1.45]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
The additivity of substrate fragments in enzyme-ligand binding., Stout TJ, Sage CR, Stroud RM, Structure. 1998 Jul 15;6(7):839-48. PMID:9687366
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