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1qml
From Proteopedia
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Revision as of 13:57, 30 October 2007
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HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE
Overview
MAD experiments attempting to solve the structure of 5--aminolaevulinic, acid dehydratase using Zn and Pb edges are described. The data obtained, proved insufficient for a complete structure solution but were invaluable, in subsequent identification of metal-binding sites using anomalous, difference Fourier analyses once the structure of the enzyme had been, solved. These sites include the highly inhibitory substitution of an, enzymic cofactor Zn(2+) ion by Pb(2+) ions, which represents a major, contribution towards understanding the molecular basis of lead poisoning., The MAD data collected at the Pb edge were also used with isomorphous, replacement data from the same Pb co-crystal and a Hg co-crystal to, provide the first delineation of the enzyme's quaternary structure. In, this MADIR ... [(full description)]
About this Structure
1QML is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HG as [ligand]. Active as [Porphobilinogen synthase], with EC number [4.2.1.24]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites., Erskine PT, Duke EM, Tickle IJ, Senior NM, Warren MJ, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):421-30. PMID:10739915
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