1y9a

From Proteopedia

(Difference between revisions)

Current revision

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate

Structural highlights

1y9a is a 2 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.81Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADH1_ENTH1 Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.^[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 apo form of alcohol dehydrogenase from a single-cell eukaryotic source, Entamoeba histolytica, has been determined at 1.8 A. To date, bacterial and archeal alcohol dehydrogenases, which are biologically active as tetramers, have crystallized with tetramers in the asymmetric unit. However, the current structure has one independent dimer per asymmetric unit and the full tetramer is generated by application of the crystallographic twofold symmetry element. This structure reveals that many of the crystallization and cryoprotection components, such as cacodylate, ethylene glycol, zinc ions and acetate, have been incorporated. These crystallization solution elements are found within the molecule and at the packing interfaces as an integral part of the three-dimensional arrangements of the tetramers. In addition, an unexpected modification of aspartic acid to O-carboxysulfanyl-4-oxo-L-homoserine was found at residue 245.

Structure of alcohol dehydrogenase from Entamoeba histolytica.,Shimon LJ, Goihberg E, Peretz M, Burstein Y, Frolow F Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):541-7. Epub 2006, Apr 19. PMID:16627948^[2]

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

References

↑ Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y. Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms. Biochemistry. 2010 Feb 9. PMID:20102159 doi:10.1021/bi901730x
↑ Shimon LJ, Goihberg E, Peretz M, Burstein Y, Frolow F. Structure of alcohol dehydrogenase from Entamoeba histolytica. Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):541-7. Epub 2006, Apr 19. PMID:16627948 doi:10.1107/S0907444906009292

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/1y9a"

@@ Line 3: / Line 3: @@
 <StructureSection load='1y9a' size='340' side='right'caption='[[1y9a]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y9a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y9A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y9a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9A FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.81&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHS:O-(CARBOXYSULFANYL)-4-OXO-L-HOMOSERINE'>OHS</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OHS:O-(CARBOXYSULFANYL)-4-OXO-L-HOMOSERINE'>OHS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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=1y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9a OCA], [https://pdbe.org/1y9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9a RCSB], [https://www.ebi.ac.uk/pdbsum/1y9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9a ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9a OCA], [http://pdbe.org/1y9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9a RCSB], [http://www.ebi.ac.uk/pdbsum/1y9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.<ref>PMID:20102159</ref>
+[https://www.uniprot.org/uniprot/ADH1_ENTH1 ADH1_ENTH1] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.<ref>PMID:20102159</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y9/1y9a_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 33: @@
 *[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
 *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
-*[[Alcohol dehydrogenase from Entamoeba histolytica|Alcohol dehydrogenase from Entamoeba histolytica]]
-*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
-*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]]
-*[[D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica|D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica]]
-*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Enthi]]
+[[Category: Entamoeba histolytica]]
 [[Category: Large Structures]]
-[[Category: Burstein, Y]]
+[[Category: Burstein Y]]
-[[Category: Frolow, F]]
+[[Category: Frolow F]]
-[[Category: Goihberg, E]]
+[[Category: Goihberg E]]
-[[Category: Peretz, M]]
+[[Category: Peretz M]]
-[[Category: Shimon, L J]]
+[[Category: Shimon LJ]]
-[[Category: Metal-binding]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]

1y9a

From Proteopedia

Current revision

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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