Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus

被引：3

作者：

Srisucharitpanit, Kanokporn ^{[1
]}

Yao, Min ^{[2
]}

Chimnaronk, Sarin ^{[1
]}

Promdonkoy, Boonhiang ^{[3
]}

Tanaka, Isao ^{[2
]}

Boonserm, Panadda ^{[1
]}

机构：

[1] Mahidol Univ, Inst Mol Biosci, Phuttamonthon 73170, Nakhon Pathom, Thailand

[2] Hokkaido Univ, Fac Adv Life Sci, Sapporo, Hokkaido 0600810, Japan

[3] Natl Sci & Technol Dev Agcy, Natl Ctr Genet Engn & Biotechnol, Klongluang 12120, Pathumthani, Thailand

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

关键词：

CULEX-PIPIENS DIPTERA; MOSQUITO LARVAE; RECEPTOR; QUINQUEFASCIATUS; DIFFRACTION; CULICIDAE; PROTEIN; MIDGUT; GUT; IDENTIFICATION;

D O I：

10.1107/S1744309113000110

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The binary toxin from Bacillus sphaericus consists of two proteins, BinA and BinB, which work together to exert toxicity against mosquito larvae. BinB is proposed to be a receptor-binding domain and internalizes BinA into the midgut cells, resulting in toxicity via an unknown mechanism. The functional form of BinB has been successfully crystallized. The crystals of BinB diffracted to a resolution of 1.75 angstrom and belong to space group P6(2)22, with unit-cell parameters a = b = 95.2, c = 154.9 angstrom. Selenomethionine-substituted BinB (SeMetBinB) was prepared and crystallized for experimental phasing. The SeMetBinB crystal data were collected at a wavelength of 0.979 angstrom and diffracted to a resolution of 1.85 angstrom.

引用

页码：170 / 173

页数：4

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