5ct6

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Wild-type Bacillus subtilis lipase A with 20% [BMIM][Cl]

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 ==Wild-type Bacillus subtilis lipase A with 20% [BMIM][Cl]==
-<StructureSection load='5ct6' size='340' side='right' caption='[[5ct6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5ct6' size='340' side='right'caption='[[5ct6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ct6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CT6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ct6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CT6 FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.902&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cri|5cri]], [[5ct4|5ct4]], [[5ct5|5ct5]], [[5ct8|5ct8]], [[5ct9|5ct9]], [[5cta|5cta]]</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></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ct6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ct6 OCA], [https://pdbe.org/5ct6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ct6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ct6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ct6 ProSAT]</span></td></tr>
-<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=5ct6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ct6 OCA], [http://pdbe.org/5ct6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ct6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ct6 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Lipase 3D Structures|Lipase 3D Structures]]
-<div class="pdbe-citations 5ct6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Triacylglycerol lipase]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Kaar, J L]]
+[[Category: Large Structures]]
-[[Category: Nordwald, E M]]
+[[Category: Kaar JL]]
-[[Category: Plaks, J G]]
+[[Category: Nordwald EM]]
-[[Category: Snell, J R]]
+[[Category: Plaks JG]]
-[[Category: Sousa, M C]]
+[[Category: Snell JR]]
-[[Category: Hydrolase]]
+[[Category: Sousa MC]]

5ct6

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Wild-type Bacillus subtilis lipase A with 20% [BMIM][Cl]

Structural highlights

Function

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