Faculté des sciences

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

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. ; Neier, Reinhard ; Cooper, J. B.

In: Acta Crystallographica Section D : Biological Crystallography, 2005, vol. 61, no. 9, p. 1222-1226

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... Plus

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    Summary
    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).