2dpg: Difference between revisions

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New page: left|200px<br /> <applet load="2dpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dpg, resolution 2.5Å" /> '''COMPLEX OF INACTIVE ...
 
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==About this Structure==
==About this Structure==
2DPG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with NAP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DPG OCA]].  
2DPG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with NAP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DPG OCA]].  


==Reference==
==Reference==
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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Revision as of 09:37, 30 October 2007

File:2dpg.gif


2dpg, resolution 2.5Å

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COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+

OverviewOverview

The catalytic mechanism of glucose 6-phosphate dehydrogenase from, Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed, mutagenesis. Each of the mutant enzymes was purified to homogeneity and, characterized by substrate binding studies and steady-state kinetic, analyses. The three-dimensional structure of the H240N glucose 6-phosphate, dehydrogenase was determined at 2.5 A resolution. The results support a, mechanism in which His-240 acts as the general base that abstracts the, proton from the C1-hydroxyl group of glucose 6-phosphate, and the, carboxylate group of Asp-177 stabilizes the positive charge that forms on, His-240 in the transition state. The results also confirm the postulated, role of ... [(full description)]

About this StructureAbout this Structure

2DPG is a [Single protein] structure of sequence from [Leuconostoc mesenteroides] with NAP as [ligand]. Active as [Oxidoreductase], with EC number [1.1.1.49]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].

ReferenceReference

On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase., Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR, Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:9485426

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OCA