3qzu

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'''Unreleased structure'''
 
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The entry 3qzu is ON HOLD
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==Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability==
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<StructureSection load='3qzu' size='340' side='right'caption='[[3qzu]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3qzu]] 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=3QZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZU FirstGlance]. <br>
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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]] 1.85&#8491;</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3qzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qzu OCA], [https://pdbe.org/3qzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qzu RCSB], [https://www.ebi.ac.uk/pdbsum/3qzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qzu ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Previously, Lipase A from Bacillus subtilis was subjected to in vitro directed evolution using iterative saturation mutagenesis, with randomization sites chosen on the basis of the highest B-factors available from the crystal structure of the wild-type (WT) enzyme. This provided mutants that, unlike WT enzyme, retained a large part of their activity after heating above 65 degrees C and cooling down. Here, we subjected the three best mutants along with the WT enzyme to biophysical and biochemical characterization. Combining thermal inactivation profiles, circular dichroism, X-ray structure analyses and NMR experiments revealed that mutations of surface amino acid residues counteract the tendency of Lipase A to undergo precipitation under thermal stress. Reduced precipitation of the unfolding intermediates rather than increased conformational stability of the evolved mutants seems to be responsible for the activity retention.
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Authors: Pijning, T., Augustyniak, W., Reetz, M.T., Dijkstra, B.W.
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Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention.,Augustyniak W, Brzezinska AA, Pijning T, Wienk H, Boelens R, Dijkstra BW, Reetz MT Protein Sci. 2012 Apr;21(4):487-97. doi: 10.1002/pro.2031. Epub 2012 Feb 29. PMID:22267088<ref>PMID:22267088</ref>
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Description: Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qzu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Lipase 3D Structures|Lipase 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Large Structures]]
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[[Category: Augustyniak W]]
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[[Category: Dijkstra BW]]
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[[Category: Pijning T]]
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[[Category: Reetz MT]]

Current revision

Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability

PDB ID 3qzu

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