1GVE
Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver
Summary for 1GVE
| Entry DOI | 10.2210/pdb1gve/pdb |
| Descriptor | AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 3, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, aldo-keto reductase, aflatoxin b1, succinic semialdehyde oxidoreductase, akr7 family |
| Biological source | RATTUS NORVEGICUS (NORWAY RAT) |
| Total number of polymer chains | 2 |
| Total formula weight | 75620.65 |
| Authors | Kozma, E.,Brown, E.,Ellis, E.M.,Lapthorn, A.J. (deposition date: 2002-02-08, release date: 2002-06-27, Last modification date: 2023-12-13) |
| Primary citation | Kozma, E.,Brown, E.,Ellis, E.M.,Lapthorn, A.J. The Crystal Structure of Rat Liver Akr7A1: A Dimeric Member of the Aldo-Keto Reductase Superfamily J.Biol.Chem., 277:16285-, 2002 Cited by PubMed Abstract: 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. PubMed: 11839745DOI: 10.1074/JBC.M110808200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.38 Å) |
Structure validation
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