4w8j

Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals

spinqualitylabelsall models 4w8j, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4w8j is a 1 chain structure with sequence from Bacillus thuringiensis serovar kurstaki str. HD73. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.78Å Ligands: CA, K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CR1AC_BACTK Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae. Publication Abstract from PubMed For almost half a century, the structure of the full-length Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac has eluded researchers, since Bt-derived crystals were first characterized in 1965. Having finally solved this structure we report intriguing details of the lattice-based interactions between the toxic core of the protein and the protoxin domains. The structure provides concrete evidence for the function of the protoxin as an enhancer of native crystal packing and stability. Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.,Evdokimov AG, Moshiri F, Sturman EJ, Rydel TJ, Zheng M, Seale JW, Franklin S Protein Sci. 2014 Nov;23(11):1491-7. doi: 10.1002/pro.2536. Epub 2014 Sep 2. PMID:25139047 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Delta-endotoxin Pesticidal crystal protein

Proteopedia Page Contributors and Editors (what is this?)

OCA