2bdx
From Proteopedia
(New page: 200px<br /> <applet load="2bdx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bdx, resolution 2.300Å" /> '''X-ray Crystal Stru...) |
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| - | [[Image:2bdx.gif|left|200px]]<br /> | + | [[Image:2bdx.gif|left|200px]]<br /><applet load="2bdx" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bdx" size=" | + | |
caption="2bdx, resolution 2.300Å" /> | caption="2bdx, resolution 2.300Å" /> | ||
'''X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1'''<br /> | '''X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The microcystins and nodularins are tumour promoting hepatotoxins that are | + | The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue. |
==About this Structure== | ==About this Structure== | ||
| - | 2BDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN and DLQ as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http:// | + | 2BDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=DLQ:'>DLQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Andersen, R | + | [[Category: Andersen, R J.]] |
| - | [[Category: Cherney, M | + | [[Category: Cherney, M M.]] |
| - | [[Category: Holmes, C | + | [[Category: Holmes, C F.]] |
| - | [[Category: James, M | + | [[Category: James, M N.]] |
| - | [[Category: Luu, H | + | [[Category: Luu, H A.]] |
| - | [[Category: Maynes, J | + | [[Category: Maynes, J T.]] |
[[Category: Williams, D.]] | [[Category: Williams, D.]] | ||
[[Category: DLQ]] | [[Category: DLQ]] | ||
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[[Category: protein phosphatase]] | [[Category: protein phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:44 2008'' |
Revision as of 14:36, 21 February 2008
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X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1
Overview
The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue.
About this Structure
2BDX is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
Reference
Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins., Maynes JT, Luu HA, Cherney MM, Andersen RJ, Williams D, Holmes CF, James MN, J Mol Biol. 2006 Feb 10;356(1):111-20. Epub 2005 Nov 22. PMID:16343532
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