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==Crystal structure of R. ruber ADH-A, mutant F43H== | |||
<StructureSection load='6ffx' size='340' side='right' caption='[[6ffx]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ffx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_sp._m8 Rhodococcus sp. m8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FFX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FFX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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">BKE56_025765 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1925550 Rhodococcus sp. M8])</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=6ffx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ffx OCA], [http://pdbe.org/6ffx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ffx RCSB], [http://www.ebi.ac.uk/pdbsum/6ffx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ffx ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Laboratory evolution of alcohol dehydrogenase produced enzyme variants with improved turnover numbers with a vicinal 1,2-diol and its corresponding hydroxyketone. Crystal structure and transient kinetics analysis aids in rationalizing the new functions of these variants. | |||
Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-diol and Its Corresponding Acyloin.,Hamnevik E, Maurer D, Enugala TR, Chu T, Lofgren R, Dobritzsch D, Widersten M Biochemistry. 2018 Feb 2. doi: 10.1021/acs.biochem.8b00055. PMID:29384657<ref>PMID:29384657</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ffx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Rhodococcus sp. m8]] | |||
[[Category: Dobritzsch, D]] | [[Category: Dobritzsch, D]] | ||
[[Category: Enugala, T R]] | |||
[[Category: Hamnevik, E]] | [[Category: Hamnevik, E]] | ||
[[Category: Maurer, D]] | |||
[[Category: Widersten, M]] | [[Category: Widersten, M]] | ||
[[Category: | [[Category: Alcohol dehydrogenase mutant variant]] | ||
[[Category: | [[Category: Nadh-dependent]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Rossmann fold]] | |||
[[Category: Zn2+-dependent]] | |||
Latest revision as of 10:20, 28 February 2018
Crystal structure of R. ruber ADH-A, mutant F43HCrystal structure of R. ruber ADH-A, mutant F43H
Structural highlights
Publication Abstract from PubMedLaboratory evolution of alcohol dehydrogenase produced enzyme variants with improved turnover numbers with a vicinal 1,2-diol and its corresponding hydroxyketone. Crystal structure and transient kinetics analysis aids in rationalizing the new functions of these variants. Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-diol and Its Corresponding Acyloin.,Hamnevik E, Maurer D, Enugala TR, Chu T, Lofgren R, Dobritzsch D, Widersten M Biochemistry. 2018 Feb 2. doi: 10.1021/acs.biochem.8b00055. PMID:29384657[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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