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5HD2

The crystal structure of SeMet-Cry51Aa2-L11M

Summary for 5HD2
Entry DOI10.2210/pdb5hd2/pdb
DescriptorParasporal crystal protein (2 entities in total)
Functional Keywordstoxin, cry51aa2, bt, cry
Biological sourceBacillus thuringiensis
Total number of polymer chains1
Total formula weight34356.02
Authors
Rydel, T.J.,Sturman, E.J.,Moshiri, F. (deposition date: 2016-01-04, release date: 2016-07-20, Last modification date: 2024-10-30)
Primary citationGowda, A.,Rydel, T.J.,Wollacott, A.M.,Brown, R.S.,Akbar, W.,Clark, T.L.,Flasinski, S.,Nageotte, J.R.,Read, A.C.,Shi, X.,Werner, B.J.,Pleau, M.J.,Baum, J.A.
A transgenic approach for controlling Lygus in cotton.
Nat Commun, 7:12213-12213, 2016
Cited by
PubMed Abstract: Lygus species of plant-feeding insects have emerged as economically important pests of cotton in the United States. These species are not controlled by commercial Bacillus thuringiensis (Bt) cotton varieties resulting in economic losses and increased application of insecticide. Previously, a Bt crystal protein (Cry51Aa2) was reported with insecticidal activity against Lygus spp. However, transgenic cotton plants expressing this protein did not exhibit effective protection from Lygus feeding damage. Here we employ various optimization strategies, informed in part by protein crystallography and modelling, to identify limited amino-acid substitutions in Cry51Aa2 that increase insecticidal activity towards Lygus spp. by >200-fold. Transgenic cotton expressing the variant protein, Cry51Aa2.834_16, reduce populations of Lygus spp. up to 30-fold in whole-plant caged field trials. One transgenic event, designated MON88702, has been selected for further development of cotton varieties that could potentially reduce or eliminate insecticide application for control of Lygus and the associated environmental impacts.
PubMed: 27426014
DOI: 10.1038/ncomms12213
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.276 Å)
Structure validation

227111

數據於2024-11-06公開中

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