5ct4: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ct4]] 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=5CT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CT4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ct4]] 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=5CT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CT4 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#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=5ct4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ct4 OCA], [https://pdbe.org/5ct4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ct4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ct4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ct4 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=5ct4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ct4 OCA], [https://pdbe.org/5ct4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ct4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ct4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ct4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>  
[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>
</div>
<div class="pdbe-citations 5ct4" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 15:21, 6 March 2024

Wild-type Bacillus subtilis lipase A with 5% [BMIM][Cl]Wild-type Bacillus subtilis lipase A with 5% [BMIM][Cl]

Structural highlights

5ct4 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.49Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESTA_BACSU Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.[1]

See Also

References

  1. ↑ Lesuisse E, Schanck K, Colson C. Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur J Biochem. 1993 Aug 15;216(1):155-60. PMID:8396026

5ct4, resolution 1.49Å

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OCA
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