Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor

L. Coates, G. Beaven, P. T. Erskine, Samuel I. Beale, S. P. Wood, P. M. Shoolingin-Jordan, J. B. Cooper

Research output: Contribution to journalArticlepeer-review

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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.

Original languageEnglish
Pages (from-to)1594-1598
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume61
Issue number12
DOIs
StatePublished - Dec 2005
Externally publishedYes

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