1gve
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of the rat liver aflatoxin dialdehyde reductase (AKR7A1) has | + | 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== | ==About this Structure== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Brown, E.]] | [[Category: Brown, E.]] | ||
| - | [[Category: Ellis, E | + | [[Category: Ellis, E M.]] |
[[Category: Kozma, E.]] | [[Category: Kozma, E.]] | ||
| - | [[Category: Lapthorn, A | + | [[Category: Lapthorn, A J.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: succinic semialdehyde oxidoreductase]] | [[Category: succinic semialdehyde oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:22 2008'' |
Revision as of 10:54, 21 February 2008
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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 with , and as ligands. Known structural/functional Site: . 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
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