1gve

From Proteopedia

(Difference between revisions)

Current revision

Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver

Structural highlights

1gve is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.38Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARK73_RAT Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. Probably involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kelly VP, Sherratt PJ, Crouch DH, Hayes JD. Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins. Biochem J. 2002 Sep 15;366(Pt 3):847-61. PMID:12071861 doi:http://dx.doi.org/10.1042/BJ20020342
↑ Kozma E, Brown E, Ellis EM, Lapthorn AJ. The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily. J Biol Chem. 2002 May 3;277(18):16285-93. Epub 2002 Feb 11. PMID:11839745 doi:10.1074/jbc.M110808200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gve"

@@ Line 1: / Line 1: @@
 ==Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver==
-<StructureSection load='1gve' size='340' side='right' caption='[[1gve]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
+<StructureSection load='1gve' size='340' side='right'caption='[[1gve]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gve]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GVE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gve]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GVE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1gve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gve RCSB], [http://www.ebi.ac.uk/pdbsum/1gve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gve ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gve OCA], [https://pdbe.org/1gve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gve RCSB], [https://www.ebi.ac.uk/pdbsum/1gve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gve ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ARK73_RAT ARK73_RAT]] Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. Probably involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.<ref>PMID:12071861</ref>
+[https://www.uniprot.org/uniprot/ARK73_RAT ARK73_RAT] Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. Probably involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.<ref>PMID:12071861</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gve_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gve_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Aldo-keto reductase|Aldo-keto reductase]]
+*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Brown, E]]
+[[Category: Large Structures]]
-[[Category: Ellis, E M]]
+[[Category: Rattus norvegicus]]
-[[Category: Kozma, E]]
+[[Category: Brown E]]
-[[Category: Lapthorn, A J]]
+[[Category: Ellis EM]]
-[[Category: Aflatoxin b1]]
+[[Category: Kozma E]]
-[[Category: Akr7 family]]
+[[Category: Lapthorn AJ]]
-[[Category: Aldo-keto reductase]]
-[[Category: Oxidoreductase]]
-[[Category: Succinic semialdehyde oxidoreductase]]

1gve

From Proteopedia

Current revision

Aflatoxin aldehyde reductase (AKR7A1) from Rat Liver

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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