1k3d
From Proteopedia
(New page: 200px<br /><applet load="1k3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3d, resolution 2.0Å" /> '''Phosphoenolpyruvate c...) |
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| - | [[Image:1k3d.jpg|left|200px]]<br /><applet load="1k3d" size=" | + | [[Image:1k3d.jpg|left|200px]]<br /><applet load="1k3d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k3d, resolution 2.0Å" /> | caption="1k3d, resolution 2.0Å" /> | ||
'''Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3'''<br /> | '''Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mechanism of reversible transfer of the gamma-phosphate group of ATP | + | The mechanism of reversible transfer of the gamma-phosphate group of ATP by Escherichia coli phosphoenolpyruvate carboxykinase (PCK) on to its substrate is of great interest. It is known that metallofluorides are accurate analogs of the transition state in the context of kinase mechanisms. Therefore, two complexes of PCK, one with AlF(3), Mg(2+) and ADP (complex I), the other with AlF(3), Mg(2+), ADP and pyruvate (complex II) were crystallized. The X-ray crystal structures of these two complexes were determined at 2.0 A resolution. The Al atom has trigonal bipyramidal geometry that mimics the transition state of phosphoryl transfer. The Al atom is at a distance of 2.8 A and 2.9 A from an oxygen atom of the beta-phosphoryl group of ADP in complex I and II, respectively. A water molecule in complex I and an oxygen atom of the pyruvate in complex II are located along the axis of the trigonal bipyramid on the side opposite to the beta-phosphoryl oxygen with respect to the equatorial plane, suggesting that the complexes are close mimics of the transition state. Along with the presence of positively charged species around the AlF(3) moiety, these results indicate that phosphoryl transfer occurs via a direct displacement mechanism with associative qualities. |
==About this Structure== | ==About this Structure== | ||
| - | 1K3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, ADP and AF3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(ATP) Phosphoenolpyruvate carboxykinase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49] Full crystallographic information is available from [http:// | + | 1K3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=AF3:'>AF3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(ATP) Phosphoenolpyruvate carboxykinase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3D OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphoenolpyruvate carboxykinase (ATP)]] | [[Category: Phosphoenolpyruvate carboxykinase (ATP)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Delbaere, L | + | [[Category: Delbaere, L T.J.]] |
[[Category: Goldie, H.]] | [[Category: Goldie, H.]] | ||
[[Category: Prasad, L.]] | [[Category: Prasad, L.]] | ||
| - | [[Category: Sudom, A | + | [[Category: Sudom, A M.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: AF3]] | [[Category: AF3]] | ||
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[[Category: nucleotide-triphosphate hydrolase.]] | [[Category: nucleotide-triphosphate hydrolase.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:37 2008'' |
Revision as of 11:29, 21 February 2008
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Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3
Overview
The mechanism of reversible transfer of the gamma-phosphate group of ATP by Escherichia coli phosphoenolpyruvate carboxykinase (PCK) on to its substrate is of great interest. It is known that metallofluorides are accurate analogs of the transition state in the context of kinase mechanisms. Therefore, two complexes of PCK, one with AlF(3), Mg(2+) and ADP (complex I), the other with AlF(3), Mg(2+), ADP and pyruvate (complex II) were crystallized. The X-ray crystal structures of these two complexes were determined at 2.0 A resolution. The Al atom has trigonal bipyramidal geometry that mimics the transition state of phosphoryl transfer. The Al atom is at a distance of 2.8 A and 2.9 A from an oxygen atom of the beta-phosphoryl group of ADP in complex I and II, respectively. A water molecule in complex I and an oxygen atom of the pyruvate in complex II are located along the axis of the trigonal bipyramid on the side opposite to the beta-phosphoryl oxygen with respect to the equatorial plane, suggesting that the complexes are close mimics of the transition state. Along with the presence of positively charged species around the AlF(3) moiety, these results indicate that phosphoryl transfer occurs via a direct displacement mechanism with associative qualities.
About this Structure
1K3D is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Phosphoenolpyruvate carboxykinase (ATP), with EC number 4.1.1.49 Full crystallographic information is available from OCA.
Reference
The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)., Sudom AM, Prasad L, Goldie H, Delbaere LT, J Mol Biol. 2001 Nov 16;314(1):83-92. PMID:11724534
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