6ffz: Difference between revisions
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==Crystal structure of R. ruber ADH-A, mutant F43H, Y54L== | |||
<StructureSection load='6ffz' size='340' side='right' caption='[[6ffz]], [[Resolution|resolution]] 1.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ffz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FFZ 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='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=6ffz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ffz OCA], [http://pdbe.org/6ffz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ffz RCSB], [http://www.ebi.ac.uk/pdbsum/6ffz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ffz 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> | |||
</div> | |||
<div class="pdbe-citations 6ffz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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]] | |||
Revision as of 09:37, 15 February 2018
Crystal structure of R. ruber ADH-A, mutant F43H, Y54LCrystal structure of R. ruber ADH-A, mutant F43H, Y54L
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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