Open AccessStructure of Chlorobium vibrioforme 5‐aminolaevulinic acid dehydratase complexed with a diacid inhibitor
Author(s) -
Coates L.,
Beaven G.,
Erskine P. T.,
Beale Samuel I.,
Wood S. P.,
ShoolinginJordan P. M.,
Cooper J. B.
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444905030350
Subject(s) - dehydratase , chemistry , stereochemistry , biochemistry , zinc , porphobilinogen synthase , active site , escherichia coli , yeast , substrate (aquarium) , enzyme , biology , organic chemistry , gene , ecology
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.