2bdx

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[[Image:2bdx.gif|left|200px]]<br /><applet load="2bdx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bdx.gif|left|200px]]
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caption="2bdx, resolution 2.300&Aring;" />
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'''X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1'''<br />
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{{Structure
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|PDB= 2bdx |SIZE=350|CAPTION= <scene name='initialview01'>2bdx</scene>, resolution 2.300&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=DLQ:DIHYDROMICROCYSTIN-LA'>DLQ</scene>
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|ACTIVITY= [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]
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|GENE= Ppp1cc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2BDX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDX OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16343532 16343532]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16343532 16343532]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Phosphoprotein phosphatase]]
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[[Category: DLQ]]
[[Category: DLQ]]
[[Category: MN]]
[[Category: MN]]
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[[Category: microcystins]]
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[[Category: microcystin]]
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[[Category: natural product inhibitors]]
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[[Category: natural product inhibitor]]
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[[Category: nodularins]]
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[[Category: nodularin]]
[[Category: protein phosphatase]]
[[Category: protein phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:00:39 2008''

Revision as of 14:00, 20 March 2008


PDB ID 2bdx

Drag the structure with the mouse to rotate
, resolution 2.300Å
Ligands: and
Gene: Ppp1cc (Homo sapiens)
Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16
Coordinates: save as pdb, mmCIF, xml



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. 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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