2bcd: Difference between revisions
New page: left|200px<br /> <applet load="2bcd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcd, resolution 2.100Å" /> '''X-ray crystal stru... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2bcd.gif|left|200px]]<br /> | [[Image:2bcd.gif|left|200px]]<br /><applet load="2bcd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2bcd" size=" | |||
caption="2bcd, resolution 2.100Å" /> | caption="2bcd, resolution 2.100Å" /> | ||
'''X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound'''<br /> | '''X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound'''<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== | ||
2BCD 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, MOQ and BME 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:// | 2BCD 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>, <scene name='pdbligand=MOQ:'>MOQ</scene> and <scene name='pdbligand=BME:'>BME</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=2BCD OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[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: BME]] | [[Category: BME]] | ||
| Line 30: | Line 29: | ||
[[Category: protein phosphtase]] | [[Category: protein phosphtase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:18 2008'' | ||
Revision as of 17:36, 21 February 2008
|
X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound
OverviewOverview
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 StructureAbout this Structure
2BCD 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.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 16:36:18 2008