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. 2018 Jan 17;84(3):e01996-17. doi: 10.1128/AEM.01996-17

FIG 3.

FIG 3

Sequence analysis of Cry64Ba and Cry64Ca proteins. (A) Multiple sequence alignments of the putative transmembrane domains (TMDs) of the Cry-ETX/MTX-like Bt toxins are shown. The putative transmembrane domain was predicted by structure simulation and is indicated by a green arrow. The hydropathy profile plot of the Cry64Ba TMD is exhibited above the amino acid sequences. The hydrophilic/hydrophobic amino acids were referred to Kyte-Doolittle methodology. Serine and threonine residues in these regions are shown in blue. (B) A phylogenetic tree of Cry proteins containing the ETX/MTX2 domain is shown. The phylogenetic tree was constructed by MEGA 7 using a neighbor-joining method with a bootstrap of 1,000 replications. (C) The simulated spatial 3D structure of Cry64Ba is shown. Cry51Aa2 (PDB code 5HD2) was selected as a model for homology modeling in SWISS-MODEL (global model quality estimation [GMQE] 0.63). Pink, α-helices; green, β-sheets; red, putative transmembrane segments. The structure was obtained by using PyMOL.