1dpg

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[[Image:1dpg.gif|left|200px]]<br /><applet load="1dpg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dpg.gif|left|200px]]
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caption="1dpg, resolution 2.0&Aring;" />
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'''GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES'''<br />
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{{Structure
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|PDB= 1dpg |SIZE=350|CAPTION= <scene name='initialview01'>1dpg</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</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= G6PD ([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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'''GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DPG 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=PO4:'>PO4</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPG OCA].
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1DPG 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=1DPG OCA].
==Reference==
==Reference==
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The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution., Rowland P, Basak AK, Gover S, Levy HR, Adams MJ, Structure. 1994 Nov 15;2(11):1073-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7881907 7881907]
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The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution., Rowland P, Basak AK, Gover S, Levy HR, Adams MJ, Structure. 1994 Nov 15;2(11):1073-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7881907 7881907]
[[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 12:19:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:10 2008''

Revision as of 08:42, 20 March 2008


PDB ID 1dpg

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands:
Gene: G6PD (Leuconostoc mesenteroides)
Activity: Glucose-6-phosphate 1-dehydrogenase, with EC number 1.1.1.49
Coordinates: save as pdb, mmCIF, xml



GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES


Overview

BACKGROUND: Glucose 6-phosphate dehydrogenase (G6PD) is the first enzyme of the pentose phosphate pathway. Normally the pathway is synthetic and NADP-dependent, but the Gram-positive bacterium Leuconostoc mesenteroides, which does not have a complete glycolytic pathway, also uses the oxidative enzymes of the pentose phosphate pathway for catabolic reactions, and selects either NAD or NADP depending on the demands for catabolic or anabolic metabolism. RESULTS: The structure of G6PD has been determined and refined to 2.0 A resolution. The enzyme is a dimer, each subunit consisting of two domains. The smaller domain is a classic dinucleotide-binding fold, while the larger one is a new beta+ alpha fold, not previously seen, with a predominantly antiparallel nine-stranded beta-sheet. There are significant structural differences in the coenzyme-binding domains of the two subunits, caused by Pro 149 which is cis in one subunit and trans in the other. CONCLUSIONS: The structure has allowed us to propose the location of the active site and the coenzyme-binding site, and suggests the role of many of the residues conserved between species. We propose that the conserved Arg46 would interact with both the adenine ring and the 2'-phosphate of NADP. Gln47, which is not conserved, may contribute to the change from NADP to dual coenzyme specificity. His178, in a nine-residue peptide conserved for all known sequences, binds a phosphate in the active site pocket. His240 is the most likely candidate for the base to oxidize the 1-hydroxyl group of the glucose 6-phosphate substrate.

About this Structure

1DPG is a Single protein structure of sequence from Leuconostoc mesenteroides. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution., Rowland P, Basak AK, Gover S, Levy HR, Adams MJ, Structure. 1994 Nov 15;2(11):1073-87. PMID:7881907

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