1gve
From Proteopedia
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==Overview== | ==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 . | + | 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== | ||
| - | 1GVE is a | + | 1GVE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAP, CIT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GVE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: succinic semialdehyde oxidoreductase]] | [[Category: succinic semialdehyde oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:45:08 2007'' |
Revision as of 12:39, 5 November 2007
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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 NAP, CIT and GOL as ligands. Structure known Active Site: AC1. 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 Mon Nov 5 14:45:08 2007
