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2dpg

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[[Image:2dpg.jpg|left|200px]]<br /><applet load="2dpg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dpg.jpg|left|200px]]
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caption="2dpg, resolution 2.5&Aring;" />
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'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''<br />
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{{Structure
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|PDB= 2dpg |SIZE=350|CAPTION= <scene name='initialview01'>2dpg</scene>, resolution 2.5&Aring;
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|SITE= <scene name='pdbsite=NUL:Active+Site+Mutant,+HIS+240+->+ASN.+The+Base+Required+To+...'>NUL</scene>
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|LIGAND= <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]
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|GENE= PLMZ/H240N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 Leuconostoc mesenteroides])
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}}
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'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] Known structural/functional Site: <scene name='pdbsite=NUL:Active+Site+Mutant,+HIS+240+->+ASN.+The+Base+Required+To+...'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPG OCA].
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2DPG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPG OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485426 9485426]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9485426 9485426]
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
[[Category: Leuconostoc mesenteroides]]
[[Category: Leuconostoc mesenteroides]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:29:51 2008''

Revision as of 14:29, 20 March 2008


PDB ID 2dpg

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites:
Ligands:
Gene: PLMZ/H240N (Leuconostoc mesenteroides)
Activity: Glucose-6-phosphate 1-dehydrogenase, with EC number 1.1.1.49
Coordinates: save as pdb, mmCIF, xml



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


Overview

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 His-178 in binding the phosphate moiety of glucose 6-phosphate.

About this Structure

2DPG is a Single protein structure of sequence from Leuconostoc mesenteroides. Full crystallographic information is available from OCA.

Reference

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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