1qml: Difference between revisions

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[[Image:1qml.jpg|left|200px]]
{{Seed}}
[[Image:1qml.png|left|200px]]


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{{STRUCTURE_1qml|  PDB=1qml  |  SCENE=  }}  
{{STRUCTURE_1qml|  PDB=1qml  |  SCENE=  }}  


'''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE'''
===HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE===




==Overview==
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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 analysis, the Hg co-crystal data were treated as native data. Anomalous difference Fouriers were again used, revealing that Hg(2+) had substituted for the same Zn(2+) cofactor ion as had Pb(2+), a finding of fundamental importance for the understanding of mercury poisoning. In addition, Pt(2+) ions were found to bind at the same place in the structure. The refined structures of the Pb- and the Hg-complexed enzymes are presented at 2.5 and 3.0 A resolution, respectively.
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{{ABSTRACT_PUBMED_10739915}}


==About this Structure==
==About this Structure==
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[[Category: Tetrapyrrole synthesis]]
[[Category: Tetrapyrrole synthesis]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
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