Article
Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus
Kanokporn Srisucharitpanit,
Min Yao,
Boonhiang Promdonkoy,
Sarin Chimnaronk,
Isao Tanaka,
Panadda Boonserm,
Kanokporn Srisucharitpanit
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Faculty of Allied Health Science, Burapha University, Saensook, Muang District, Chon Buri, 20131 Thailand
Search for more papers by this authorMin Yao
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, 060-0810 Japan
Search for more papers by this authorBoonhiang Promdonkoy
National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Pahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani, 12120 Thailand
Search for more papers by this authorSarin Chimnaronk
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Search for more papers by this authorCorresponding Author
Isao Tanaka
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, 060-0810 Japan
Correspondence to: Isao Tanaka, Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060–0810, Japan. E-mail: [email protected] and Panadda Boonserm, Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand. E-mail: [email protected]Search for more papers by this authorCorresponding Author
Panadda Boonserm
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Correspondence to: Isao Tanaka, Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060–0810, Japan. E-mail: [email protected] and Panadda Boonserm, Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand. E-mail: [email protected]Search for more papers by this authorKanokporn Srisucharitpanit,
Min Yao,
Boonhiang Promdonkoy,
Sarin Chimnaronk,
Isao Tanaka,
Panadda Boonserm,
Kanokporn Srisucharitpanit
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Faculty of Allied Health Science, Burapha University, Saensook, Muang District, Chon Buri, 20131 Thailand
Search for more papers by this authorMin Yao
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, 060-0810 Japan
Search for more papers by this authorBoonhiang Promdonkoy
National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Pahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani, 12120 Thailand
Search for more papers by this authorSarin Chimnaronk
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Search for more papers by this authorCorresponding Author
Isao Tanaka
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, 060-0810 Japan
Correspondence to: Isao Tanaka, Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060–0810, Japan. E-mail: [email protected] and Panadda Boonserm, Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand. E-mail: [email protected]Search for more papers by this authorCorresponding Author
Panadda Boonserm
Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom, 73170 Thailand
Correspondence to: Isao Tanaka, Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060–0810, Japan. E-mail: [email protected] and Panadda Boonserm, Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand. E-mail: [email protected]Search for more papers by this authorABSTRACT
The binary toxin (Bin), produced by Lysinibacillus sphaericus, is composed of BinA (42 kDa) and BinB (51 kDa) proteins, which are both required for full toxicity against Culex and Anopheles mosquito larvae. Specificity of Bin toxin is determined by the binding of BinB component to a receptor present on the midgut epithelial membranes, while BinA is proposed to be a toxic component. Here, we determined the first crystal structure of the active form of BinB at a resolution of 1.75 Å. BinB possesses two distinct structural domains in its N- and C-termini. The globular N-terminal domain has a β-trefoil scaffold which is a highly conserved architecture of some sugar binding proteins or lectins, suggesting a role of this domain in receptor-binding. The BinB β-rich C-terminal domain shares similar three-dimensional folding with aerolysin type β-pore forming toxins, despite a low sequence identity. The BinB structure, therefore, is a new member of the aerolysin-like toxin family, with probably similarities in the cytolytic mechanism that takes place via pore formation. Proteins 2014; 82:2703–2712. © 2014 Wiley Periodicals, Inc.
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