2c1h: Difference between revisions

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==Overview==
==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.
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==
Line 17: Line 17:
[[Category: Beaven, G.]]
[[Category: Beaven, G.]]
[[Category: Coates, L.]]
[[Category: Coates, L.]]
[[Category: Cooper, J.B.]]
[[Category: Cooper, J B.]]
[[Category: Erskine, P.T.]]
[[Category: Erskine, P T.]]
[[Category: Shoolingin-Jordan, P.M.]]
[[Category: Shoolingin-Jordan, P M.]]
[[Category: Wood, S.P.]]
[[Category: Wood, S P.]]
[[Category: DSB]]
[[Category: DSB]]
[[Category: MG]]
[[Category: MG]]
Line 30: Line 30:
[[Category: porphyrin biosynthesis]]
[[Category: porphyrin biosynthesis]]


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Revision as of 14:43, 21 February 2008

File:2c1h.jpg


2c1h, resolution 2.60Å

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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 MG and DSB as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: AC1. 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

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