2dpg
From Proteopedia
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|PDB= 2dpg |SIZE=350|CAPTION= <scene name='initialview01'>2dpg</scene>, resolution 2.5Å | |PDB= 2dpg |SIZE=350|CAPTION= <scene name='initialview01'>2dpg</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=NUL:Active+Site+Mutant,+HIS+240+->+ASN.+The+Base+Required+To+...'>NUL</scene> | |SITE= <scene name='pdbsite=NUL:Active+Site+Mutant,+HIS+240+->+ASN.+The+Base+Required+To+...'>NUL</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene> | + | |LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= PLMZ/H240N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 Leuconostoc mesenteroides]) | |GENE= PLMZ/H240N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 Leuconostoc mesenteroides]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpg OCA], [http://www.ebi.ac.uk/pdbsum/2dpg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpg RCSB]</span> | ||
}} | }} | ||
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[[Category: Naylor, C E.]] | [[Category: Naylor, C E.]] | ||
[[Category: Paludin, S.]] | [[Category: Paludin, S.]] | ||
| - | [[Category: NAP]] | ||
[[Category: choh(d) - nad(p)]] | [[Category: choh(d) - nad(p)]] | ||
[[Category: glucose metabolism]] | [[Category: glucose metabolism]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:39 2008'' |
Revision as of 23:37, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Gene: | PLMZ/H240N (Leuconostoc mesenteroides) | ||||||
| Activity: | Glucose-6-phosphate 1-dehydrogenase, with EC number 1.1.1.49 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 02:37:39 2008
