1o08
From Proteopedia
(New page: 200px<br /><applet load="1o08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o08, resolution 1.20Å" /> '''Structure of Pentava...) |
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| - | [[Image:1o08.gif|left|200px]]<br /><applet load="1o08" size=" | + | [[Image:1o08.gif|left|200px]]<br /><applet load="1o08" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o08, resolution 1.20Å" /> | caption="1o08, resolution 1.20Å" /> | ||
'''Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate'''<br /> | '''Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymes provide enormous rate enhancements, unmatched by any other type of | + | Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate. |
==About this Structure== | ==About this Structure== | ||
| - | 1O08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with G16 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] Full crystallographic information is available from [http:// | + | 1O08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with <scene name='pdbligand=G16:'>G16</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O08 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allen, K | + | [[Category: Allen, K N.]] |
[[Category: Dunaway-Mariano, D.]] | [[Category: Dunaway-Mariano, D.]] | ||
| - | [[Category: Lahiri, S | + | [[Category: Lahiri, S D.]] |
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
[[Category: G16]] | [[Category: G16]] | ||
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[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:57 2008'' |
Revision as of 12:12, 21 February 2008
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Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate
Overview
Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.
About this Structure
1O08 is a Single protein structure of sequence from Lactococcus lactis with and as ligands. Active as Beta-phosphoglucomutase, with EC number 5.4.2.6 Full crystallographic information is available from OCA.
Reference
The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction., Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN, Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13. PMID:12637673
Page seeded by OCA on Thu Feb 21 14:11:57 2008
