This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5cri

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:21, 6 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]==
==Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]==
-
<StructureSection load='5cri' size='340' side='right' caption='[[5cri]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
+
<StructureSection load='5cri' size='340' side='right'caption='[[5cri]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5cri]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CRI FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5cri]] 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=5CRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CRI FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.63&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cri OCA], [http://pdbe.org/5cri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cri RCSB], [http://www.ebi.ac.uk/pdbsum/5cri PDBsum]</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=5cri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cri OCA], [https://pdbe.org/5cri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cri RCSB], [https://www.ebi.ac.uk/pdbsum/5cri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cri ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[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>
-
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 5cri" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Triacylglycerol lipase]]
+
[[Category: Bacillus subtilis]]
-
[[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]]
-
[[Category: Wild-type]]
+

Current revision

Wild-type Bacillus subtilis lipase A with 0% [BMIM][Cl]

PDB ID 5cri

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5cri"
Personal tools