5o9d: Difference between revisions

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New page: '''Unreleased structure''' The entry 5o9d is ON HOLD until Paper Publication Authors: Dobritzsch, D., Maurer, D., Hamnevik, E., Enugala, T.R., Widersten, M. Description: Crystal struct...
 
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'''Unreleased structure'''


The entry 5o9d is ON HOLD  until Paper Publication
==Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, Y54F, F43H, H39Y==
<StructureSection load='5o9d' size='340' side='right'caption='[[5o9d]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5o9d]] is a 4 chain structure with sequence from [https://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=5O9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O9D 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]] 1.79&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9ON:(2~{S})-2-methylpentanedioic+acid'>9ON</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5o9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9d OCA], [https://pdbe.org/5o9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o9d RCSB], [https://www.ebi.ac.uk/pdbsum/5o9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1Q8I6M1_9NOCA A0A1Q8I6M1_9NOCA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alcohol dehydrogenase A (ADH-A) from Rhodococcus ruber DSM 44541 is a promising biocatalyst for redox transformations of arylsubstituted sec-alcohols and ketones. The enzyme is stereoselective in the oxidation of 1-phenylethanol with a 300-fold preference for the (S)-enantiomer. The low catalytic efficiency with (R)-1-phenylethanol has been attributed to nonproductive binding of this substrate at the active site. Aiming to modify the enantioselectivity, to rather favor the (R)-alcohol, and also test the possible involvement of nonproductive substrate binding as a mechanism in substrate discrimination, we performed directed laboratory evolution of ADH-A. Three targeted sites that contribute to the active-site cavity were exposed to saturation mutagenesis in a stepwise manner and the generated variants were selected for improved catalytic activity with (R)-1-phenylethanol. After three subsequent rounds of mutagenesis, selection and structure-function analysis of isolated ADH-A variants, we conclude: (1) W295 has a key role as a structural determinant in the discrimination between (R)- and (S)-1-phenylethanol and a W295A substitution fundamentally changes the stereoselectivity of the protein. One observable effect is a faster rate of NADH release, which changes the rate-limiting step of the catalytic cycle from coenzyme release to hydride transfer. (2) The obtained change in enantiopreference, from the (S)- to the (R)-alcohol, can be partly explained by a shift in the nonproductive substrate binding modes. This article is protected by copyright. All rights reserved.


Authors: Dobritzsch, D., Maurer, D., Hamnevik, E., Enugala, T.R., Widersten, M.
Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a non-preferred alcohol enantiomer.,Hamnevik E, Enugala TR, Maurer D, Ntuku S, Oliveira A, Dobritzsch D, Widersten M FEBS J. 2017 Sep 30. doi: 10.1111/febs.14279. PMID:28963762<ref>PMID:28963762</ref>


Description: Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, Y54F, F43H, H39Y
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hamnevik, E]]
<div class="pdbe-citations 5o9d" style="background-color:#fffaf0;"></div>
[[Category: Widersten, M]]
 
[[Category: Enugala, T.R]]
==See Also==
[[Category: Maurer, D]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
[[Category: Dobritzsch, D]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus sp. M8]]
[[Category: Dobritzsch D]]
[[Category: Enugala TR]]
[[Category: Hamnevik E]]
[[Category: Maurer D]]
[[Category: Widersten M]]
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