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Structure of yeast 5-aminolevulinic acid dehydratase complexed with the inhibitor 5-hydroxylevulinic acid
Auteur(s)
Erskine, P. T.
Coates, L.
Newbold, R.
Brindley, A. A.
Stauffer, Frederic
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 Crystallogr., Sect. D Biol. Crystallogr.
Vol.
9
No
D61
De la page
1222
A la page
1226
Mots-clés
- Yeast (crystal structure of yeast 5-aminolevulinate dehydratase complexed with 5-hydroxylevulinic acid)
- Enzyme functional sites (inhibitor-binding
- of 5-aminolevulinate dehydratase of yeast)
- Crystal growth
- Crystal structure (of 5-aminolevulinate dehydratase of yeast complexed with 5-hydroxylevulinic acid)
- Conformation (protein
- of 5-aminolevulinate dehydratase of yeast complexed with 5-hydroxylevulinic acid)
- aminolevulinate dehydratase yeast hydroxylevulinate complex crystal structure
Résumé
The x-ray crystal structure of 5-aminolevulinate dehydratase (ALAD) of yeast complexed with the competitive inhibitor, 5-hydroxylevulinic acid, was detd. at a resoln. of 1.9 Å. The structure showed that the inhibitor was bound by a Schiff-base link to one of the invariant active site Lys residues (Lys-263). The inhibitor appeared to bind in 2 well-defined conformations and the interactions made by it suggested that it is a very close analog of the substrate, 5-aminolevulinic acid (ALA). [on SciFinder(R)]
Identifiants
Type de publication
journal article
