5ct5: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 5ct5 is ON HOLD
+==Wild-type Bacillus subtilis lipase A with 10% [BMIM][Cl]==
+<StructureSection load='5ct5' size='340' side='right'caption='[[5ct5]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ct5]] is a 2 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=5CT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CT5 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]] 1.747&#8491;</td></tr>
+<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ct5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ct5 OCA], [https://pdbe.org/5ct5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ct5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ct5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ct5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Erik Nordwald, Joseph Plaks, Marcelo Sousa, Joel Kaar
+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>
-Description: Wild-type lipase A from Bacillus subtilis resolved with 0 % v/v [BMIM][Cl]
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Erik Nordwald, Joseph Plaks, Marcelo Sousa, Joel Kaar]]
+<div class="pdbe-citations 5ct5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Lipase 3D Structures|Lipase 3D Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bacillus subtilis]]
+[[Category: Large Structures]]
+[[Category: Kaar JL]]
+[[Category: Nordwald EM]]
+[[Category: Plaks JG]]
+[[Category: Snell JR]]
+[[Category: Sousa MC]]