4eez: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eez]] 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=4EEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eez]] 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=4EEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEZ 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]] 1.9&#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=4eez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eez OCA], [https://pdbe.org/4eez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eez RCSB], [https://www.ebi.ac.uk/pdbsum/4eez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eez 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=4eez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eez OCA], [https://pdbe.org/4eez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eez RCSB], [https://www.ebi.ac.uk/pdbsum/4eez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eez 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 4eez" 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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 11:03, 1 March 2024

Crystal Structure of Lactococcus lactis Alcohol Dehydrogenase variant RE1

4eez, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA