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1gve

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[[Image:1gve.jpg|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gve OCA], [http://www.ebi.ac.uk/pdbsum/1gve PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gve RCSB]</span>
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'''AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER'''
'''AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER'''
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[[Category: Kozma, E.]]
[[Category: Kozma, E.]]
[[Category: Lapthorn, A J.]]
[[Category: Lapthorn, A J.]]
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[[Category: aflatoxin b1]]
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[[Category: Aflatoxin b1]]
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[[Category: akr7 family]]
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[[Category: Akr7 family]]
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[[Category: aldo-keto reductase]]
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[[Category: Aldo-keto reductase]]
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[[Category: succinic semialdehyde oxidoreductase]]
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[[Category: Succinic semialdehyde oxidoreductase]]
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Revision as of 15:03, 2 May 2008

Template:STRUCTURE 1gve

AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER


Overview

The structure of the rat liver aflatoxin dialdehyde reductase (AKR7A1) has been solved to 1.38-A resolution. Although it shares a similar alpha/beta-barrel structure with other members of the aldo-keto reductase superfamily, AKR7A1 is the first dimeric member to be crystallized. The crystal structure also reveals details of the ternary complex as one subunit of the dimer contains NADP(+) and the inhibitor citrate. Although the underlying catalytic mechanism appears similar to other aldo-keto reductases, the substrate-binding pocket contains several charged amino acids (Arg-231 and Arg-327) that distinguish it from previously characterized aldo-keto reductases with respect to size and charge. These differences account for the substrate specificity for 4-carbon acid-aldehydes such as succinic semialdehyde and 2-carboxybenzaldehyde as well as for the idiosyncratic substrate aflatoxin B(1) dialdehyde of this subfamily of enzymes. Structural differences between the AKR7A1 ternary complex and apoenzyme reveal a significant hinged movement of the enzyme involving not only the loops of the structure but also parts of the alpha/beta-barrel most intimately involved in cofactor binding.

About this Structure

1GVE is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily., Kozma E, Brown E, Ellis EM, Lapthorn AJ, J Biol Chem. 2002 May 3;277(18):16285-93. Epub 2002 Feb 11. PMID:11839745 Page seeded by OCA on Fri May 2 18:03:25 2008

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