2C1H

The X-ray Structure of Chlorobium vibrioforme 5-Aminolaevulinic Acid Dehydratase Complexed with a Diacid Inhibitor

Summary for 2C1H

• Entry DOI: 10.2210/pdb2c1h/pdb
• Related: 1W1Z
• Descriptor: DELTA-AMINOLEVULINIC ACID DEHYDRATASE, MAGNESIUM ION, 4,7-DIOXOSEBACIC ACID, ... (4 entities in total)
• Functional Keywords: lyase, alad, 5-aminolaevulinic acid dehydratase, heme biosynthesis, magnesium, porphyrin biosynthesis
• Biological source: CHLOROBIUM VIBRIOFORME
• Total number of polymer chains: 2
• Total formula weight: 73378.09

Authors

Coates, L.,Beaven, G.,Erskine, P.T.,Beale, S.,Wood, S.P.,Shoolingin-Jordan, P.M.,Cooper, J.B. (deposition date: 2005-09-14, release date: 2005-12-02, Last modification date: 2023-12-13)

Primary citation

Coates, L.,Beaven, G.,Erskine, P.T.,Beale, S.,Wood, S.P.,Shoolingin-Jordan, P.M.,Cooper, J.B.
Structure of Chlorobium Vibrioforme 5-Aminolaevulinic Acid Dehydratase Complexed with a Diacid Inhibitor.
Acta Crystallogr.,Sect.D, 61:1594-, 2005

PubMed Abstract: 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.

PubMed: 16304458
DOI: 10.1107/S0907444905030350

Experimental method

X-RAY DIFFRACTION (2.6 Å)