1hw6: Difference between revisions
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|PDB= 1hw6 |SIZE=350|CAPTION= <scene name='initialview01'>1hw6</scene>, resolution 1.90Å | |PDB= 1hw6 |SIZE=350|CAPTION= <scene name='initialview01'>1hw6</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1a80|1A80]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw6 OCA], [http://www.ebi.ac.uk/pdbsum/1hw6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hw6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Blaber, M.]] | [[Category: Blaber, M.]] | ||
[[Category: Sanli, G.]] | [[Category: Sanli, G.]] | ||
[[Category: aldo-keto reductase]] | [[Category: aldo-keto reductase]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:14 2008'' | ||
Revision as of 21:11, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1A80
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE
OverviewOverview
A 1.9 A resolution X-ray structure of the apo-form of Corynebacterium 2,5-diketo-d-gluconic acid reductase A (2,5-DKGR A), a member of the aldo-keto reductase superfamily, has been determined by molecular replacement using the NADPH-bound form of the same enzyme as the search model. 2,5-DKGR A catalyzes the NADPH-dependent stereo-specific reduction of 2,5-diketo-d-gluconate (2,5-DKG) to 2-keto-l-gulonate, a precursor in the industrial production of vitamin C. An atomic-resolution structure for the apo-form of the enzyme, in conjunction with our previously reported high-resolution X-ray structure for the holo-enzyme and holo/substrate model, allows a comparative analysis of structural changes that accompany cofactor binding. The results show that regions of the active site undergo coordinated conformational changes of up to 8 A. These conformational changes result in the organization and structural rearrangement of residues associated with substrate binding and catalysis. Thus, NADPH functions not only to provide a hydride ion for catalytic reduction, but is also a critical structural component for formation of a catalytically competent form of DKGR A.
About this StructureAbout this Structure
1HW6 is a Single protein structure of sequence from Corynebacterium sp.. Full crystallographic information is available from OCA.
ReferenceReference
Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor., Sanli G, Blaber M, J Mol Biol. 2001 Jun 22;309(5):1209-18. PMID:11399090
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