2c1h
From Proteopedia
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==Overview== | ==Overview== | ||
- | The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase | + | 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== | ==About this Structure== | ||
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[[Category: Beaven, G.]] | [[Category: Beaven, G.]] | ||
[[Category: Coates, L.]] | [[Category: Coates, L.]] | ||
- | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
- | [[Category: Erskine, P | + | [[Category: Erskine, P T.]] |
- | [[Category: Shoolingin-Jordan, P | + | [[Category: Shoolingin-Jordan, P M.]] |
- | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
[[Category: DSB]] | [[Category: DSB]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: porphyrin biosynthesis]] | [[Category: porphyrin biosynthesis]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:54 2008'' |
Revision as of 14:43, 21 February 2008
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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 Thu Feb 21 16:43:54 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