1fjm

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(New page: 200px<br /> <applet load="1fjm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjm, resolution 2.1&Aring;" /> '''PROTEIN SERINE/THREO...)
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[[Image:1fjm.gif|left|200px]]<br /><applet load="1fjm" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1fjm" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1fjm, resolution 2.1&Aring;" />
caption="1fjm, resolution 2.1&Aring;" />
'''PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN'''<br />
'''PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN'''<br />
==Overview==
==Overview==
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The crystal structure of mammalian protein phosphatase-1, complexed with, the toxin microcystin and determined at 2.1 A resolution, reveals that it, is a metalloenzyme unrelated in architecture to the tyrosine phosphatases., Two metal ions are positioned by a central beta-alpha-beta-alpha-beta, scaffold at the active site, from which emanate three surface grooves that, are potential binding sites for substrates and inhibitors. The carboxy, terminus is positioned at the end of one of the grooves such that, regulatory sequences following the domain might modulate function. The, fold of the catalytic domain is expected to be closely preserved in, protein phosphatases 2A and 2B (calcineurin).
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The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).
==About this Structure==
==About this Structure==
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1FJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Microcystis_aeruginosa Microcystis aeruginosa] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJM OCA].
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1FJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Microcystis_aeruginosa Microcystis aeruginosa] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MN:'>MN</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=1FJM OCA].
==Reference==
==Reference==
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[[Category: Goldberg, J.]]
[[Category: Goldberg, J.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
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[[Category: Nairn, A.C.]]
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[[Category: Nairn, A C.]]
[[Category: BME]]
[[Category: BME]]
[[Category: MN]]
[[Category: MN]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:53:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:20 2008''

Revision as of 10:39, 21 February 2008


1fjm, resolution 2.1Å

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PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN

Overview

The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).

About this Structure

1FJM is a Single protein structure of sequence from Microcystis aeruginosa and Oryctolagus cuniculus with and as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1., Goldberg J, Huang HB, Kwon YG, Greengard P, Nairn AC, Kuriyan J, Nature. 1995 Aug 31;376(6543):745-53. PMID:7651533

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