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==Cry3Aa protein for enzyme entrapment== | ==Cry3Aa protein for enzyme entrapment== | ||
<StructureSection load='6lfp' size='340' side='right'caption='[[6lfp]]' scene=''> | <StructureSection load='6lfp' size='340' side='right'caption='[[6lfp]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LFP OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6lfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LFP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.31Å</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=6lfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lfp OCA], [https://pdbe.org/6lfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lfp RCSB], [https://www.ebi.ac.uk/pdbsum/6lfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lfp ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CR3AA_BACTD CR3AA_BACTD] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cry3Aa is a protein that forms crystals naturally in the bacterium Bacillus thuringiensis. Here we report that coexpression of Cry3Aa and a Proteus mirabilis lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications. | |||
In Vivo Enzyme Entrapment in a Protein Crystal.,Heater BS, Yang Z, Lee MM, Chan MK J Am Chem Soc. 2020 Jun 3;142(22):9879-9883. doi: 10.1021/jacs.9b13462. Epub 2020, May 19. PMID:32407637<ref>PMID:32407637</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lfp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Pesticidal crystal protein|Pesticidal crystal protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus thuringiensis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chan MK]] | [[Category: Chan MK]] | ||
[[Category: Heater BS]] | [[Category: Heater BS]] | ||
Latest revision as of 13:59, 22 November 2023
Cry3Aa protein for enzyme entrapmentCry3Aa protein for enzyme entrapment
Structural highlights
FunctionCR3AA_BACTD Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. Publication Abstract from PubMedCry3Aa is a protein that forms crystals naturally in the bacterium Bacillus thuringiensis. Here we report that coexpression of Cry3Aa and a Proteus mirabilis lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications. In Vivo Enzyme Entrapment in a Protein Crystal.,Heater BS, Yang Z, Lee MM, Chan MK J Am Chem Soc. 2020 Jun 3;142(22):9879-9883. doi: 10.1021/jacs.9b13462. Epub 2020, May 19. PMID:32407637[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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