1b8j: Difference between revisions
New page: left|200px<br /><applet load="1b8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8j, resolution 1.90Å" /> '''ALKALINE PHOSPHATASE... |
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[[Image:1b8j.gif|left|200px]]<br /><applet load="1b8j" size=" | [[Image:1b8j.gif|left|200px]]<br /><applet load="1b8j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1b8j, resolution 1.90Å" /> | caption="1b8j, resolution 1.90Å" /> | ||
'''ALKALINE PHOSPHATASE COMPLEXED WITH VANADATE'''<br /> | '''ALKALINE PHOSPHATASE COMPLEXED WITH VANADATE'''<br /> | ||
==Overview== | ==Overview== | ||
A high resolution crystal structure of Escherichia coli alkaline | A high resolution crystal structure of Escherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 A resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction. | ||
==About this Structure== | ==About this Structure== | ||
1B8J 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 ZN, SO4 and MG 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:// | 1B8J 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=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</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=1B8J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Holtz, K | [[Category: Holtz, K M.]] | ||
[[Category: Kantrowitz, E | [[Category: Kantrowitz, E R.]] | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: vanadate]] | [[Category: vanadate]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:39 2008'' | ||
Revision as of 12:52, 21 February 2008
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ALKALINE PHOSPHATASE COMPLEXED WITH VANADATE
OverviewOverview
A high resolution crystal structure of Escherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 A resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction.
About this StructureAbout this Structure
1B8J is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Alkaline phosphatase, with EC number 3.1.3.1 Full crystallographic information is available from OCA.
ReferenceReference
A model of the transition state in the alkaline phosphatase reaction., Holtz KM, Stec B, Kantrowitz ER, J Biol Chem. 1999 Mar 26;274(13):8351-4. PMID:10085061
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