1ofb
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CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH MANGANESE(II)
OverviewOverview
3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthases are, metal-dependent enzymes that catalyse the first committed step in the, biosynthesis of aromatic amino acids in microorganisms and plants, the, condensation of 2-phophoenolpyruvate (PEP) and d-erythrose 4-phosphate, (E4P) to DAHP. The DAHP synthases are possible targets for fungicides and, represent a model system for feedback regulation in metabolic pathways. To, gain further insight into the role of the metal ion and the catalytic, mechanism in general, the crystal structures of several complexes between, the tyrosine-regulated form of DAHP synthase from Saccharomyces cerevisiae, and different metal ions and ligands have been determined. The crystal, structures provide evidence that the simultaneous presence of a metal ... [(full description)]
About this StructureAbout this Structure
1OFB is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with MN and GOL as [ligands]. Active as [Transferred entry: 2.5.1.54], with EC number [4.1.2.15]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Substrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism., Konig V, Pfeil A, Braus GH, Schneider TR, J Mol Biol. 2004 Mar 26;337(3):675-90. PMID:15019786
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