2c1h
From Proteopedia
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THE X-RAY STRUCTURE OF CHLOROBIUM VIBRIOFORME 5-AMINOLAEVULINIC ACID DEHYDRATASE COMPLEXED WITH A DIACID INHIBITOR
Overview
The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase, (ALAD) complexed with the irreversible inhibitor 4,7-dioxosebacic acid has, been solved. The inhibitor binds by forming Schiff-base linkages with, lysines 200 and 253 at the active site. The structure reported here, provides a definition of the interactions made by both of the substrate, molecules (A-side and P-side substrates) with the C. vibrioforme ALAD and, is compared and contrasted with structures of the same inhibitor bound to, Escherichia coli and yeast ALAD. The structure suggests why, 4,7-dioxosebacic acid is a better inhibitor of the zinc-dependent ALADs, than of the zinc-independent ALADs.
About this Structure
2C1H is a Single protein structure of sequence from Prosthecochloris vibrioformis with and as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor., Coates L, Beaven G, Erskine PT, Beale SI, Wood SP, Shoolingin-Jordan PM, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1594-8. Epub 2005, Nov 19. PMID:16304458
Page seeded by OCA on Sun Feb 3 10:30:18 2008
Categories: Porphobilinogen synthase | Prosthecochloris vibrioformis | Single protein | Beale, S. | Beaven, G. | Coates, L. | Cooper, J.B. | Erskine, P.T. | Shoolingin-Jordan, P.M. | Wood, S.P. | DSB | MG | 5-aminolaevulinic acid dehydratase | Alad | Heme biosynthesis | Lyase | Magnesium | Porphyrin biosynthesis
