1qnv

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[[Image:1qnv.jpg|left|200px]]<br /><applet load="1qnv" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qnv.jpg|left|200px]]
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caption="1qnv, resolution 2.5&Aring;" />
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'''YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE LEAD (PB) COMPLEX'''<br />
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{{Structure
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|PDB= 1qnv |SIZE=350|CAPTION= <scene name='initialview01'>1qnv</scene>, resolution 2.5&Aring;
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|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene>
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|LIGAND= <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene>
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|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]
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|GENE=
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}}
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'''YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE LEAD (PB) COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QNV 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 <scene name='pdbligand=PB:'>PB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1QMK. 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+Site'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNV OCA].
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1QNV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry 1QMK. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNV OCA].
==Reference==
==Reference==
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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]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:14 2008''

Revision as of 11:40, 20 March 2008


PDB ID 1qnv

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites:
Ligands:
Activity: Porphobilinogen synthase, with EC number 4.2.1.24
Coordinates: save as pdb, mmCIF, xml



YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE LEAD (PB) COMPLEX


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

1QNV is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 1QMK. 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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