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Mosquito‐larvicidal binary toxin receptor protein (Cqm1): crystallization and X‐ray crystallographic analysis
Author(s) -
Sharma Mahima,
Lakshmi Ashwitha,
Gupta Gagan D.,
Kumar Vinay
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18010671
Subject(s) - pore forming toxin , toxin , crystallization , crystallography , chemistry , biology , microbiology and biotechnology , microbial toxins , organic chemistry
Cqm1 from Culex quinquefasciatus has been identified as the receptor for Lysinibacillus sphaericus binary toxin (BinAB). It is an amylomaltase that is presented on the epithelial membrane in the larval midgut through a glycosyl‐phosphatidylinositol anchor. The active core of this protein (residues 23–560) was overexpressed in Escherichia coli , purified and successfully crystallized by the sitting‐drop vapor‐diffusion method using d ‐arabinose and CaCl 2 as additives, as identified using high‐throughput differential scanning fluorimetry analysis. X‐ray diffraction data were collected to a resolution of 2.8 Å using a laboratory X‐ray source. The crystals had the symmetry of space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 191.3, b = 205.3, c = 59.0 Å and with four monomers in the asymmetric unit. Structure refinement is in progress. This is the first structure report for a binary toxin receptor and for a member of the GH13_17 subfamily in the CAZy database.