1hw6: Difference between revisions
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[[Image:1hw6.jpg|left|200px]] | [[Image:1hw6.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE''' | {{Structure | ||
|PDB= 1hw6 |SIZE=350|CAPTION= <scene name='initialview01'>1hw6</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HW6 is a [ | 1HW6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW6 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11399090 11399090] | ||
[[Category: Corynebacterium sp.]] | [[Category: Corynebacterium sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:42:22 2008'' | ||
Revision as of 12:42, 20 March 2008
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| 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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