1qml
From Proteopedia
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| - | [[Image:1qml.jpg|left|200px]] | + | [[Image:1qml.jpg|left|200px]] |
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| - | '''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE''' | + | {{Structure |
| + | |PDB= 1qml |SIZE=350|CAPTION= <scene name='initialview01'>1qml</scene>, resolution 3.0Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Catalytic+Residues'>CAT</scene> | ||
| + | |LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QML is a [ | + | 1QML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/10739915 10739915] |
[[Category: Porphobilinogen synthase]] | [[Category: Porphobilinogen synthase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:50 2008'' |
Revision as of 11:39, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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