title: Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus.
abstract: 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 Å and belong to space group P6(2)22, with unit-cell parameters a = b = 95.2, c = 154.9 Å. Selenomethionine-substituted BinB (SeMetBinB) was prepared and crystallized for experimental phasing. The SeMetBinB crystal data were collected at a wavelength of 0.979 Å and diffracted to a resolution of 1.85 Å.
authors: Institute of Molecular Biosciences, Mahidol University, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand.
authors: Kanokporn
authors: K
authors: Srisucharitpanit
authors: Min
authors: M
authors: Yao
authors: Sarin
authors: S
authors: Chimnaronk
authors: Boonhiang
authors: B
authors: Promdonkoy
authors: Isao
authors: I
authors: Tanaka
authors: Panadda
authors: P
authors: Boonserm
mesh_terms: D001407:Bacillus / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D001427:Bacterial Toxins; C046134:binB protein, Bacillus sphaericus
keywords: Bacillus sphaericus; BinB; SAD; binary toxin; mosquito-larvicidal toxin
references: J Mol Biol. 1966 Mar;16(1):118-33
references: 5331240
references: J Invertebr Pathol. 2011 Feb;106(2):230-5
references: 20965197
references: Insect Biochem Mol Biol. 1999 Aug;29(8):711-21
references: 10451923
references: Appl Environ Microbiol. 1987 Jun;53(6):1333-7
references: 2886104
references: Can J Microbiol. 1990 Nov;36(11):804-7
references: 1980629
references: FEMS Microbiol Lett. 2010 Feb;303(1):84-91
references: 20002193
references: J Invertebr Pathol. 1997 May;69(3):197-204
references: 9170345
references: J Gen Microbiol. 1992 Jul;138(7):1515-26
references: 1512580
references: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):271-81
references: 21460445
references: BMB Rep. 2011 Oct;44(10):674-9
references: 22027002
references: Acta Crystallogr A. 2008 Jan;64(Pt 1):112-22
references: 18156677
references: Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1083-5
references: 10216313
references: Microbiol Rev. 1991 Sep;55(3):425-36
references: 1682792
references: FEMS Microbiol Lett. 2011 Aug;321(2):167-74
references: 21645049
references: Biochem Biophys Res Commun. 2006 Apr 21;342(4):1273-8
references: 16516147
references: Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):952-3
references: 15103150
references: J Bacteriol. 1993 Jan;175(2):510-8
references: 8419297
references: Cell Microbiol. 2005 Sep;7(9):1335-44
references: 16098220
references: Science. 1992 Nov 6;258(5084):987-91
references: 1279805
references: Protein Expr Purif. 2012 Apr;82(2):368-72
references: 22381463
references: J Membr Biol. 2001 Nov 15;184(2):171-83
references: 11719853
references: Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1413-20
references: 11053839
references: J Mol Biol. 1968 Apr 28;33(2):491-7
references: 5700707
references: Insect Biochem Mol Biol. 2001 Sep;31(10):981-90
references: 11483434
references: Annu Rev Entomol. 1996;41:451-72
references: 15012337