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6lfp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cry3Aa protein for enzyme entrapment== | |
| + | <StructureSection load='6lfp' size='340' side='right'caption='[[6lfp]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | == 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> | |
| - | [[Category: | + | </div> |
| - | [[Category: Chan | + | <div class="pdbe-citations 6lfp" style="background-color:#fffaf0;"></div> |
| - | [[Category: Heater | + | |
| + | ==See Also== | ||
| + | *[[Pesticidal crystal protein|Pesticidal crystal protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus thuringiensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chan MK]] | ||
| + | [[Category: Heater BS]] | ||
Current revision
Cry3Aa protein for enzyme entrapment
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