1ed8

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[[Image:1ed8.gif|left|200px]]<br /><applet load="1ed8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ed8.gif|left|200px]]
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caption="1ed8, resolution 1.75&Aring;" />
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'''STRUCTURE OF E. COLI ALKALINE PHOSPHATASE INHIBITED BY THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION'''<br />
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{{Structure
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|PDB= 1ed8 |SIZE=350|CAPTION= <scene name='initialview01'>1ed8</scene>, resolution 1.75&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]
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|GENE=
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}}
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'''STRUCTURE OF E. COLI ALKALINE PHOSPHATASE INHIBITED BY THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ED8 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=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED8 OCA].
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1ED8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED8 OCA].
==Reference==
==Reference==
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A revised mechanism for the alkaline phosphatase reaction involving three metal ions., Stec B, Holtz KM, Kantrowitz ER, J Mol Biol. 2000 Jun 23;299(5):1303-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873454 10873454]
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A revised mechanism for the alkaline phosphatase reaction involving three metal ions., Stec B, Holtz KM, Kantrowitz ER, J Mol Biol. 2000 Jun 23;299(5):1303-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10873454 10873454]
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: wild type]]
[[Category: wild type]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:58 2008''

Revision as of 08:54, 20 March 2008

Image:1ed8.gif


PDB ID 1ed8

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: , , and
Activity: Alkaline phosphatase, with EC number 3.1.3.1
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF E. COLI ALKALINE PHOSPHATASE INHIBITED BY THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION


Overview

Here, X-ray crystallography has been used to investigate the proposed double in-line displacement mechanism of Escherichia coli alkaline phosphatase in which two of the three active-site metal ions have a direct role in catalysis. Two new X-ray crystal structures of the wild-type enzyme in the absence and presence of inorganic phosphate have been refined at 1.75 A to final working R-factors of 15.4% and 16.4%, respectively. In the refinement of both structures, residues in the active sites were treated anisotropically. The ellipsoids resulting from the partial anisotropic refinement show a clear route for the binding and release of substrate/product. In addition, a direct comparison of the refined structures with and without phosphate reveal a strong correlation between the occupancy of the third metal-binding site and the conformation of the Ser102 nucleophile. These findings clarify two important and unresolved aspects of the previously proposed catalytic mechanism, how Ser102 is activated for nucleophilic attack and why a magnesium ion in the third metal site is required for catalysis. Analysis of these results suggest that three metal-ion assisted catalysis is a more accurate description of the mechanism of the alkaline phosphatase reaction. A revised mechanism for the catalytic reaction of alkaline phosphatase is proposed on the basis of the two new X-ray crystal structures reported.

About this Structure

1ED8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A revised mechanism for the alkaline phosphatase reaction involving three metal ions., Stec B, Holtz KM, Kantrowitz ER, J Mol Biol. 2000 Jun 23;299(5):1303-11. PMID:10873454

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