6lfp

From Proteopedia

Cry3Aa protein for enzyme entrapment

Structural highlights

6lfp is a 1 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.31Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CR3AA_BACTD Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations

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References

↑ Heater BS, Yang Z, Lee MM, Chan MK. In Vivo Enzyme Entrapment in a Protein Crystal. J Am Chem Soc. 2020 Jun 3;142(22):9879-9883. PMID:32407637 doi:10.1021/jacs.9b13462