National Bureau of Agriculturally Important Microorganisms (ICAR), Kusmaur, Kaithauli, Mau Nath Bhanjan, 275101 India.
Indian J Microbiol. 2012 Jun;52(2):263-9. doi: 10.1007/s12088-011-0191-5. Epub 2011 Jun 26.
The first theoretical structural model of newly reported Cry1Ab16 δ-endotoxin produced by Bacillus thuringiensis AC11 was predicted using homology modeling technique. Cry1Ab16 resembles the Cry1Aa protein structure by sharing a common three domains structure responsible in pore forming and specificity determination along with few structural deviations. The main differences between the two is in the length of loops, absence of α7b, α9a, α10b, α11a and presence of additional β12b, α13 components while α10a is spatially located at downstream position in Cry1Ab16. A better understanding of the 3D structure shall be helpful in the design of domain swapping and mutagenesis experiments aimed at improving toxicity.
利用同源建模技术，预测了新报道的苏云金芽孢杆菌 AC11 产生的 Cry1Ab16 δ-内毒素的首个理论结构模型。Cry1Ab16 与 Cry1Aa 蛋白结构相似，具有共同的负责形成孔和特异性确定的三个结构域，以及一些结构差异。两者之间的主要区别在于环的长度、缺失 α7b、α9a、α10b、α11a 和存在额外的β12b、α13 成分，而α10a 在 Cry1Ab16 中位于下游位置。更好地了解 3D 结构将有助于设计旨在提高毒性的结构域交换和诱变实验。
