1it6
From Proteopedia
(New page: 200px<br /> <applet load="1it6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1it6, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1it6.gif|left|200px]]<br /> | + | [[Image:1it6.gif|left|200px]]<br /><applet load="1it6" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1it6" size=" | + | |
caption="1it6, resolution 2.0Å" /> | caption="1it6, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1'''<br /> | '''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the catalytic subunit of the protein phosphatase | + | The crystal structure of the catalytic subunit of the protein phosphatase 1 (PP1), PP1 gamma, in complex with a marine toxin, calyculin A, was determined at 2.0 A resolution. The metal binding site contains the phosphate group of calyculin A and forms a tight network via the hydrophilic interactions between PP1 and calyculin A. Calyculin A is located in two of the three grooves, namely, in the hydrophobic groove and the acidic groove on the molecular surface. This is the first observation to note that the inhibitor adopts not a pseudocyclic conformation but an extended conformation in order to form a complex with the protein. The amino acid terminus of calyculin A contributes, in a limited manner, to the binding to PP1 gamma, which is consistent with findings from the studies of dose-inhibition analysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1IT6 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 CYU 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:// | + | 1IT6 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=CYU:'>CYU</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=1IT6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase-inhibitor complex]] | [[Category: hydrolase-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:23 2008'' |
Revision as of 11:15, 21 February 2008
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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1
Overview
The crystal structure of the catalytic subunit of the protein phosphatase 1 (PP1), PP1 gamma, in complex with a marine toxin, calyculin A, was determined at 2.0 A resolution. The metal binding site contains the phosphate group of calyculin A and forms a tight network via the hydrophilic interactions between PP1 and calyculin A. Calyculin A is located in two of the three grooves, namely, in the hydrophobic groove and the acidic groove on the molecular surface. This is the first observation to note that the inhibitor adopts not a pseudocyclic conformation but an extended conformation in order to form a complex with the protein. The amino acid terminus of calyculin A contributes, in a limited manner, to the binding to PP1 gamma, which is consistent with findings from the studies of dose-inhibition analysis.
About this Structure
1IT6 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 structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1., Kita A, Matsunaga S, Takai A, Kataiwa H, Wakimoto T, Fusetani N, Isobe M, Miki K, Structure. 2002 May;10(5):715-24. PMID:12015153
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