1ynq

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[[Image:1ynq.gif|left|200px]]<br /><applet load="1ynq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ynq.gif|left|200px]]
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caption="1ynq, resolution 1.300&Aring;" />
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'''aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)'''<br />
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{{Structure
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|PDB= 1ynq |SIZE=350|CAPTION= <scene name='initialview01'>1ynq</scene>, resolution 1.300&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE= BH1011 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=86665 Bacillus halodurans])
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}}
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'''aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YNQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NDP:'>NDP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNQ OCA].
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1YNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNQ OCA].
==Reference==
==Reference==
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High-resolution crystal structure of AKR11C1 from Bacillus halodurans: an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase., Marquardt T, Kostrewa D, Balakrishnan R, Gasperina A, Kambach C, Podjarny A, Winkler FK, Balendiran GK, Li XD, J Mol Biol. 2005 Nov 25;354(2):304-16. Epub 2005 Oct 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16242712 16242712]
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High-resolution crystal structure of AKR11C1 from Bacillus halodurans: an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase., Marquardt T, Kostrewa D, Balakrishnan R, Gasperina A, Kambach C, Podjarny A, Winkler FK, Balendiran GK, Li XD, J Mol Biol. 2005 Nov 25;354(2):304-16. Epub 2005 Oct 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16242712 16242712]
[[Category: Bacillus halodurans]]
[[Category: Bacillus halodurans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: akr11c1]]
[[Category: akr11c1]]
[[Category: aldo-keto reductase]]
[[Category: aldo-keto reductase]]
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[[Category: bacillus halodurans]]
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[[Category: bacillus haloduran]]
[[Category: nadph]]
[[Category: nadph]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:12 2008''

Revision as of 13:25, 20 March 2008

Image:1ynq.gif


PDB ID 1ynq

Drag the structure with the mouse to rotate
, resolution 1.300Å
Ligands: , , , and
Gene: BH1011 (Bacillus halodurans)
Coordinates: save as pdb, mmCIF, xml



aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)


Overview

Aldo-keto reductase AKR11C1 from Bacillus halodurans, a new member of aldo-keto reductase (AKR) family 11, has been characterized structurally and biochemically. The structures of the apo and NADPH bound form of AKR11C1 have been solved to 1.25 A and 1.3 A resolution, respectively. AKR11C1 possesses a novel non-aromatic stacking interaction of an arginine residue with the cofactor, which may favor release of the oxidized cofactor. Our biochemical studies have revealed an NADPH-dependent activity of AKR11C1 with 4-hydroxy-2,3-trans-nonenal (HNE). HNE is a cytotoxic lipid peroxidation product, and detoxification in alkaliphilic bacteria, such as B.halodurans, plays a crucial role in survival. AKR11C1 could thus be part of the detoxification system, which ensures the well being of the microorganism. The very poor activity of AKR11C1 on standard, small substrates such as benzaldehyde or DL-glyeraldehyde is consistent with the observed, very open active site lacking a binding pocket for these substrates. In contrast, modeling of HNE with its aldehyde function suitably positioned in the active site suggests that its elongated hydrophobic tail occupies a groove defined by hydrophobic side-chains. Multiple sequence alignment of AKR11C1 with the highly homologous iolS and YqkF proteins shows a high level of conservation in this putative substrate-binding site. We suggest that AKR11C1 is the first structurally characterized member of a new class of AKRs with specificity for substrates with long aliphatic tails.

About this Structure

1YNQ is a Single protein structure of sequence from Bacillus halodurans. Full crystallographic information is available from OCA.

Reference

High-resolution crystal structure of AKR11C1 from Bacillus halodurans: an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase., Marquardt T, Kostrewa D, Balakrishnan R, Gasperina A, Kambach C, Podjarny A, Winkler FK, Balendiran GK, Li XD, J Mol Biol. 2005 Nov 25;354(2):304-16. Epub 2005 Oct 10. PMID:16242712

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