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Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid
Auteur(s)
Erskine, P. T.
Coates, L.
Newbold, R.
Brindley, A. A.
Stauffer, Frédéric
Beaven, G. D. E.
Gill, R.
Coker, A.
Wood, S. P.
Warren, M. J.
Shoolingin-Jordan, P. M.
Cooper, J. B.
Date de parution
2005
In
Acta Crystallographica Section D : Biological Crystallography, International Union of Crystallography, 2005/61/9/1222-1226
Résumé
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 Å. 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).
Identifiants
Type de publication
journal article
