View source for 4ure


==Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1==
<StructureSection load='4ure' size='340' side='right'caption='[[4ure]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ure]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aromatoleum_aromaticum_EbN1 Aromatoleum aromaticum EbN1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4URE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PS:3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE'>1PS</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ure FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ure OCA], [https://pdbe.org/4ure PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ure RCSB], [https://www.ebi.ac.uk/pdbsum/4ure PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ure ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5P8S7_AROAE Q5P8S7_AROAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The dehydrogenation of 1-(4-hydroxyphenyl)-ethanol to 4-hydroxyacetophenone represents the second reaction step during anaerobic degradation of p-ethylphenol in the denitrifying bacterium 'Aromatoleum aromaticum' EbN1. Previous proteogenomic studies identified two different proteins (ChnA and EbA309) as possible candidates for catalyzing this reaction [Wohlbrand et al: J Bacteriol 2008;190:5699-5709]. Physiological-molecular characterization of newly generated unmarked in-frame deletion and complementation mutants allowed defining ChnA (renamed here as Hped) as the enzyme responsible for 1-(4-hydroxyphenyl)-ethanol oxidation. Hped [1-(4-hydroxyphenyl)-ethanol dehydrogenase] belongs to the 'classical' family within the short-chain alcohol dehydrogenase/reductase (SDR) superfamily. Hped was overproduced in Escherichia coli, purified and crystallized. The X-ray structures of the apo- and NAD+-soaked form were resolved at 1.5 and 1.1 A, respectively, and revealed Hped as a typical homotetrameric SDR. Modeling of the substrate 4-hydroxyacetophenone (reductive direction of Hped) into the active site revealed the structural determinants of the strict (R)-specificity of Hped (Phe187), contrasting the (S)-specificity of previously reported 1-phenylethanol dehydrogenase (Ped; Tyr93) from strain EbN1 [Hoffken et al: Biochemistry 2006;45:82-93].

Molecular Genetic and Crystal Structural Analysis of 1-(4-Hydroxyphenyl)-Ethanol Dehydrogenase from 'Aromatoleum aromaticum' EbN1.,Busing I, Hoffken HW, Breuer M, Wohlbrand L, Hauer B, Rabus R J Mol Microbiol Biotechnol. 2015;25(5):327-39. doi: 10.1159/000439113. Epub 2015 , Oct 22. PMID:26488297<ref>PMID:26488297</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ure" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aromatoleum aromaticum EbN1]]
[[Category: Large Structures]]
[[Category: Breuer M]]
[[Category: Buesing I]]
[[Category: Hauer B]]
[[Category: Hoeffken HW]]
[[Category: Rabus R]]
[[Category: Woehlbrand L]]