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1qml
From Proteopedia
(New page: 200px<br /> <applet load="1qml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qml, resolution 3.0Å" /> '''HG COMPLEX OF YEAST ...) |
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QML OCA]]. | + | 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]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QML OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10739915 10739915] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10739915 10739915] | ||
| + | [[Category: Porphobilinogen synthase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Oct 30 14:27:25 2007'' |
Revision as of 12:22, 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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