1s95
From Proteopedia
(New page: 200px<br /> <applet load="1s95" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s95, resolution 1.60Å" /> '''Structure of serine...) |
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| - | [[Image:1s95.gif|left|200px]]<br /> | + | [[Image:1s95.gif|left|200px]]<br /><applet load="1s95" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1s95" size=" | + | |
caption="1s95, resolution 1.60Å" /> | caption="1s95, resolution 1.60Å" /> | ||
'''Structure of serine/threonine protein phosphatase 5'''<br /> | '''Structure of serine/threonine protein phosphatase 5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Serine/threonine protein phosphatase-5 (PP5) affects many signaling | + | Serine/threonine protein phosphatase-5 (PP5) affects many signaling networks that regulate cell growth and cellular responses to stress. Here we report the crystal structure of the PP5 catalytic domain (PP5c) at a resolution of 1.6 A. From this structure we propose a mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a conserved Asp271-M1:M2-W1-His427-His304-Asp274 catalytic motif (where M1 and M2 are metals and W1 is a water molecule). The structure of PP5c provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases, which are among the most powerful known catalysts. Resolution of the entire C terminus revealed a novel subdomain, and the structure of the PP5c should also aid development of type-specific inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1S95 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, PO4 and MPD 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:// | + | 1S95 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=PO4:'>PO4</scene> and <scene name='pdbligand=MPD:'>MPD</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=1S95 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ciszak, E | + | [[Category: Ciszak, E M.]] |
| - | [[Category: Honkanen, R | + | [[Category: Honkanen, R E.]] |
| - | [[Category: Swingle, M | + | [[Category: Swingle, M R.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
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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 14:59:11 2008'' |
Revision as of 12:59, 21 February 2008
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Structure of serine/threonine protein phosphatase 5
Overview
Serine/threonine protein phosphatase-5 (PP5) affects many signaling networks that regulate cell growth and cellular responses to stress. Here we report the crystal structure of the PP5 catalytic domain (PP5c) at a resolution of 1.6 A. From this structure we propose a mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a conserved Asp271-M1:M2-W1-His427-His304-Asp274 catalytic motif (where M1 and M2 are metals and W1 is a water molecule). The structure of PP5c provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases, which are among the most powerful known catalysts. Resolution of the entire C terminus revealed a novel subdomain, and the structure of the PP5c should also aid development of type-specific inhibitors.
About this Structure
1S95 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
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5., Swingle MR, Honkanen RE, Ciszak EM, J Biol Chem. 2004 Aug 6;279(32):33992-9. Epub 2004 May 23. PMID:15155720
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