4eex: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_KF147 Lactococcus lactis subsp. lactis KF147]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEX FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_KF147 Lactococcus lactis subsp. lactis KF147]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=4eex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eex OCA], [https://pdbe.org/4eex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eex RCSB], [https://www.ebi.ac.uk/pdbsum/4eex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eex ProSAT]</span></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=4eex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eex OCA], [https://pdbe.org/4eex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eex RCSB], [https://www.ebi.ac.uk/pdbsum/4eex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eex ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/D2BLA0_LACLK D2BLA0_LACLK]]
[https://www.uniprot.org/uniprot/D2BLA0_LACLK D2BLA0_LACLK]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the X-ray crystal structures of the NADH-dependent alcohol dehydrogenase LlAdhA from Lactococcus lactis and its laboratory-evolved variant LlAdhA(RE1) at 1.9A and 2.5A resolution, respectively. LlAdhA(RE1), which contains three amino acid mutations (Y50F, I212T, and L264V), was engineered to increase the microbial production of isobutanol (2-methylpropan-1-ol) from isobutyraldehyde (2-methylpropanal). Structural comparison of LlAdhA and LlAdhA(RE1) indicates that the enhanced activity on isobutyraldehyde stems from increases in the protein's active site size, hydrophobicity, and substrate access. Further structure-guided mutagenesis generated a quadruple mutant (Y50F/N110S/I212T/L264V), whose K(M) for isobutyraldehyde is approximately 17-fold lower and catalytic efficiency (k(cat)/K(M)) is approximately 160-fold higher than wild-type LlAdhA. Combining detailed structural information and directed evolution, we have achieved significant improvements in non-native alcohol dehydrogenase activity that will facilitate the production of next-generation fuels such as isobutanol from renewable resources.
 
Structure-guided engineering of Lactococcus lactis alcohol dehydrogenase LlAdhA for improved conversion of isobutyraldehyde to isobutanol.,Liu X, Bastian S, Snow CD, Brustad EM, Saleski TE, Xu JH, Meinhold P, Arnold FH J Biotechnol. 2012 Sep 3. pii: S0168-1656(12)00610-4. doi:, 10.1016/j.jbiotec.2012.08.008. PMID:22974724<ref>PMID:22974724</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4eex" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>
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