1qml
From Proteopedia
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| - | [[Image:1qml. | + | [[Image:1qml.jpg|left|200px]]<br /><applet load="1qml" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qml" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1qml, resolution 3.0Å" /> | caption="1qml, resolution 3.0Å" /> | ||
'''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE'''<br /> | '''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] | + | 1QML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic Residues'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QML OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:57:22 2007'' |
Revision as of 15:47, 18 December 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 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.
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 Known structural/functional Site: . 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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