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

被引：5

作者：

Erskine, PT

Coates, L

Newbold, R

Brindley, AA

Stauffer, F

Beaven, GDE

Gill, R

Coker, A

Wood, SP

Warren, MJ

Shoolingin-Jordan, PM

Neier, R

Cooper, JB

机构：

[1] Univ Southampton, Sch Biol Sci, Southampton SO16 7PX, Hants, England

[2] Univ London, QueenMary, Sch Biol Sci, London E1 4NS, England

[3] Univ Neuchatel, Inst Chim, CH-2007 Neuchatel, Switzerland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷

关键词：

D O I：

10.1107/S0907444905018834

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom. 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).

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页码：1222 / 1226

页数：5

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