View source for 6iqd


==Crystal structure of Alcohol dehydrogenase from Geobacillus stearothermophilus==
<StructureSection load='6iqd' size='340' side='right'caption='[[6iqd]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iqd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IQD 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]] 2.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6iqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqd OCA], [https://pdbe.org/6iqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iqd RCSB], [https://www.ebi.ac.uk/pdbsum/6iqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADH2_GEOSE ADH2_GEOSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. When an NAD-dependent ADH oxidizes methanol, albeit at a poor rate, it may be treated as methanol dehydrogenase (MDH). One ADH from Geobacillus stearothermophilus DSM 2334 (GsADH) has been widely used as MDH, but its actual substrate scope remains less characterized. Here we purified recombinant GsADH from Escherichia coli and determined its crystal structure. We collected kinetics data of this enzyme towards a number of short chain alcohols, and found that isopropanol is by far the most favorable substrate. Moreover, molecular docking analysis suggested that substrate preference is mainly attributed to the conformer energy of the protein-substrate complex. Our data clarified the substrate scope of GsADH and provided structural insights, which may facilitate more efficient cofactor regeneration and rational metabolic engineering.

Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase.,Guo X, Feng Y, Wang X, Liu Y, Liu W, Li Q, Wang J, Xue S, Zhao ZK Bioorg Med Chem Lett. 2019 Jun 15;29(12):1446-1449. doi:, 10.1016/j.bmcl.2019.04.025. Epub 2019 Apr 16. PMID:31006524<ref>PMID:31006524</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iqd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Feng Y]]
[[Category: Guo X]]
[[Category: Xue S]]
[[Category: Zhao Z]]