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

نویسندگان

  • P T Erskine
  • L Coates
  • R Newbold
  • A A Brindley
  • F Stauffer
  • G D E Beaven
  • R Gill
  • A Coker
  • S P Wood
  • M J Warren
  • P M Shoolingin-Jordan
  • R Neier
  • J B Cooper
چکیده

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 A. 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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عنوان ژورنال:
  • Acta crystallographica. Section D, Biological crystallography

دوره 61 Pt 9  شماره 

صفحات  -

تاریخ انتشار 2005