Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

P. T. Erskine, L. Coates, R. Newbold, A. A. Brindley, F. Stauffer, G. D. E. Beaven, R. Gill, A. Coker, S. P. Wood, M. J. Warren, P. M. Shoolingin-Jordan, R. Neier, J. B. Cooper

Research output: Contribution to journalArticlepeer-review

Abstract

The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).

Original languageEnglish
Pages (from-to)1222-6
Number of pages5
JournalActa Crystallographica Section D
VolumeD61
Issue numberPt 9
DOIs
Publication statusPublished - Sep 2005

Keywords

  • Aminolevulinic Acid/analogs & derivatives
  • Binding Sites
  • Crystallography, X-Ray
  • Fungal Proteins/chemistry
  • Molecular Structure
  • Porphobilinogen Synthase/antagonists & inhibitors
  • Protein Conformation
  • Schiff Bases

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