5cur

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==G158E/K44E/R57E/Y49E Bacillus subtilis lipase A with 20% [BMIM][Cl]==
==G158E/K44E/R57E/Y49E Bacillus subtilis lipase A with 20% [BMIM][Cl]==
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<StructureSection load='5cur' size='340' side='right' caption='[[5cur]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='5cur' size='340' side='right'caption='[[5cur]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5cur]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CUR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CUR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5cur]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BM0:1-BUTYL-3-METHYL-1H-IMIDAZOL-3-IUM'>BM0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.302&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cri|5cri]], [[5ct4|5ct4]], [[5ct5|5ct5]], [[5ct6|5ct6]], [[5ct8|5ct8]], [[5ct9|5ct9]], [[5cta|5cta]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BM0:1-BUTYL-3-METHYL-1H-IMIDAZOL-3-IUM'>BM0</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cur OCA], [https://pdbe.org/5cur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cur RCSB], [https://www.ebi.ac.uk/pdbsum/5cur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cur ProSAT]</span></td></tr>
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<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=5cur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cur OCA], [http://pdbe.org/5cur PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cur RCSB], [http://www.ebi.ac.uk/pdbsum/5cur PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ESTA_BACSU ESTA_BACSU] Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.<ref>PMID:8396026</ref>
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We present the first crystallographic insight into the interactions of an ionic liquid (IL) with an enzyme, which has widespread implications for stabilizing enzymes in IL media for biocatalysis. Structures of Bacillus subtilis lipase A (lipA) and an IL-stable variant (QM-lipA) were obtained in the presence of increasing concentrations of 1-butyl-3-methylimidazolium chloride ([BMIM][Cl]). These studies revealed that the [BMIM] cation interacts with surface residues through hydrophobic and cation-pi interactions. Of specific interest was the disruption of internal stacking interactions of aromatic side chains by [BMIM], which provides structural evidence for the mechanism of enzyme denaturation by ILs. The interaction of [BMIM] and Cl ions with lipA was reduced by the stabilizing mutations Y49E and G158E in QM-lipA. Ultimately, these findings present the molecular basis for stabilizing enzymes from IL-induced inactivation, as well as the selection of ILs that are less denaturing.
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Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.,Nordwald EM, Plaks JG, Snell JR, Sousa MC, Kaar JL Chembiochem. 2015 Nov;16(17):2456-9. doi: 10.1002/cbic.201500398. Epub 2015 Oct, 14. PMID:26388426<ref>PMID:26388426</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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<div class="pdbe-citations 5cur" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Triacylglycerol lipase]]
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[[Category: Bacillus subtilis]]
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[[Category: Kaar, J L]]
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[[Category: Large Structures]]
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[[Category: Nordwald, E M]]
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[[Category: Kaar JL]]
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[[Category: Plaks, J G]]
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[[Category: Nordwald EM]]
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[[Category: Snell, J R]]
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[[Category: Plaks JG]]
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[[Category: Sousa, M C]]
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[[Category: Snell JR]]
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[[Category: Hydrolase]]
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[[Category: Sousa MC]]

Current revision

G158E/K44E/R57E/Y49E Bacillus subtilis lipase A with 20% [BMIM][Cl]

PDB ID 5cur

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