1gve
From Proteopedia
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| - | [[Image:1gve. | + | [[Image:1gve.jpg|left|200px]]<br /><applet load="1gve" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gve" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gve, resolution 1.38Å" /> | caption="1gve, resolution 1.38Å" /> | ||
'''AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER'''<br /> | '''AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. | + | 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]. Known structural/functional Site: <scene name='pdbsite=AC1:Cit Binding Site For Chain A'>AC1</scene>. 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 Tue Dec 18 15:39:13 2007'' |
Revision as of 13:29, 18 December 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. 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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