Smulevitch S V, Osterman A L, Shevelev A B, Kaluger S V, Karasin A I, Kadyrov R M, Zagnitko O P, Chestukhina G G, Stepanov V M
Institute of Microbial Genetics, Lab. of Protein Chemistry, Moscow, USSR.
FEBS Lett. 1991 Nov 18;293(1-2):25-8. doi: 10.1016/0014-5793(91)81144-w.
A gene cryIg coding for entomocidal protein delta-endotoxin of Bacillus thuringiensis ssp. galleriae str. 11-67 named CryIG has been cloned and sequenced (EMBL accession number X58120). The deduced amino acid sequence that contains 1156 amino acid residues shows only 28% of identical residues, when compared with other delta-endotoxins of the CryI family. The extent of identity is substantially higher for some regions of the sequence ('conserved blocks'), that presumably bear important structural or functional properties. This implies that CryIG delta-endotoxin follows the same type of polypeptide chain folding as other CryI proteins, whereas peculiarities of primary structure help to explain its unique specificity.
已克隆并测序了编码苏云金芽孢杆菌蜡螟亚种菌株11 - 67的杀虫蛋白δ-内毒素的cryIg基因（命名为CryIG）（EMBL登录号X58120）。推导的包含1156个氨基酸残基的氨基酸序列与CryI家族的其他δ-内毒素相比，仅有28%的相同残基。对于该序列的某些区域（“保守区段”），相同程度要高得多，这些区域可能具有重要的结构或功能特性。这意味着CryIGδ-内毒素与其他CryI蛋白遵循相同类型的多肽链折叠方式，而一级结构的特殊性有助于解释其独特的特异性。
