1qml

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[[Image:1qml.jpg|left|200px]]
[[Image:1qml.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1qml |SIZE=350|CAPTION= <scene name='initialview01'>1qml</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1qml", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:Catalytic+Residues'>CAT</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1qml| PDB=1qml | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qml OCA], [http://www.ebi.ac.uk/pdbsum/1qml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qml RCSB]</span>
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}}
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'''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE'''
'''HG COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE'''
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[[Category: Warren, M J.]]
[[Category: Warren, M J.]]
[[Category: Wood, S P.]]
[[Category: Wood, S P.]]
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[[Category: aldolase]]
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[[Category: Aldolase]]
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[[Category: dehydratase]]
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[[Category: Dehydratase]]
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[[Category: tetrapyrrole synthesis]]
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[[Category: Tetrapyrrole synthesis]]
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[[Category: tim barrel]]
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[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:27:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:55 2008''
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Revision as of 03:27, 3 May 2008

Template:STRUCTURE 1qml

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 Page seeded by OCA on Sat May 3 06:27:15 2008

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