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.

doi:10.1107/S0907444905018834

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

Author(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.

Neier, Reinhard

Institut de chimie

Cooper, J. B.

Date issued

2005

In

Acta Crystallographica Section D : Biological Crystallography, International Union of Crystallography, 2005/61/9/1222-1226

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 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).