1h7n
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SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH LAEVULINIC ACID AT 1.6 A RESOLUTION
OverviewOverview
The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with, substrate (5-aminolaevulinic acid) and three inhibitors: laevulinic acid, succinylacetone and 4-keto-5-aminolaevulinic acid, have been solved at, high resolution. The ligands all bind by forming a covalent link with, Lys263 at the active site. The structures define the interactions made by, one of the two substrate moieties that bind to the enzyme during, catalysis. All of the inhibitors induce a significant ordering of the flap, covering the active site. Succinylacetone appears to be unique by inducing, a number of conformational changes in loops covering the active site, which may be important for understanding the co-operative properties of, ALAD enzymes. Succinylacetone is produced in large amounts by ... [(full description)]
About this StructureAbout this Structure
1H7N is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with ZN and SHF as [ligands]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].
ReferenceReference
The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors., Erskine PT, Newbold R, Brindley AA, Wood SP, Shoolingin-Jordan PM, Warren MJ, Cooper JB, J Mol Biol. 2001 Sep 7;312(1):133-41. PMID:11545591
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