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| | ==Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus== | | ==Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus== |
| - | <StructureSection load='3wa1' size='340' side='right' caption='[[3wa1]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3wa1' size='340' side='right'caption='[[3wa1]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wa1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14577 Atcc 14577]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WA1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WA1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wa1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WA1 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">binB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1421 ATCC 14577])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wa1 OCA], [http://pdbe.org/3wa1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wa1 RCSB], [http://www.ebi.ac.uk/pdbsum/3wa1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wa1 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wa1 OCA], [https://pdbe.org/3wa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wa1 RCSB], [https://www.ebi.ac.uk/pdbsum/3wa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wa1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BINB2_LYSSH BINB2_LYSSH] Component of a binary toxin active against Culex and some Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). This subunit is responsible for localized binding to specific regions of the host larval gut. The individual subunits are not toxic. BinAB and this subunit alone bind to the gastric caecum and posterior midgut of C.quinquefasciatus larvae. Binary toxin internalization into host gut cells requires both proteins. Does not bind to the midgut of Aedes aegypti (PubMed:1512580). Toxic to Aedes atropalpus mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). Binding component of binary toxin. The 51 kDa polypeptide acts synergetically with the 42 kDa polypeptide for expression of a larvicidal toxin.<ref>PMID:1512580</ref> <ref>PMID:8419297</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14577]] | + | [[Category: Large Structures]] |
| - | [[Category: Boonserm, P]] | + | [[Category: Lysinibacillus sphaericus]] |
| - | [[Category: Chimnaronk, S]] | + | [[Category: Boonserm P]] |
| - | [[Category: Promdonkoy, B]] | + | [[Category: Chimnaronk S]] |
| - | [[Category: Srisucharitpanit, K]] | + | [[Category: Promdonkoy B]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Srisucharitpanit K]] |
| - | [[Category: Yao, M]] | + | [[Category: Tanaka I]] |
| - | [[Category: A-b toxin]]
| + | [[Category: Yao M]] |
| - | [[Category: Binary toxin]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
BINB2_LYSSH Component of a binary toxin active against Culex and some Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). This subunit is responsible for localized binding to specific regions of the host larval gut. The individual subunits are not toxic. BinAB and this subunit alone bind to the gastric caecum and posterior midgut of C.quinquefasciatus larvae. Binary toxin internalization into host gut cells requires both proteins. Does not bind to the midgut of Aedes aegypti (PubMed:1512580). Toxic to Aedes atropalpus mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). Binding component of binary toxin. The 51 kDa polypeptide acts synergetically with the 42 kDa polypeptide for expression of a larvicidal toxin.[1] [2]
Publication Abstract from PubMed
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 A. BinB possesses two distinct structural domains in its N- and C-termini. The globular N-terminal domain has a beta-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 beta-rich C-terminal domain shares similar three-dimensional folding with aerolysin type beta-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. (c) 2014 Wiley Periodicals, Inc.
Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus.,Srisucharitpanit K, Yao M, Promdonkoy B, Chimnaronk S, Tanaka I, Boonserm P Proteins. 2014 Oct;82(10):2703-12. doi: 10.1002/prot.24636. Epub 2014 Jul 5. PMID:24975613[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oei C, Hindley J, Berry C. Binding of purified Bacillus sphaericus binary toxin and its deletion derivatives to Culex quinquefasciatus gut: elucidation of functional binding domains. J Gen Microbiol. 1992 Jul;138(7):1515-26. PMID:1512580 doi:10.1099/00221287-138-7-1515
- ↑ Berry C, Hindley J, Ehrhardt AF, Grounds T, de Souza I, Davidson EW. Genetic determinants of host ranges of Bacillus sphaericus mosquito larvicidal toxins. J Bacteriol. 1993 Jan;175(2):510-8. PMID:8419297 doi:10.1128/jb.175.2.510-518.1993
- ↑ Srisucharitpanit K, Yao M, Promdonkoy B, Chimnaronk S, Tanaka I, Boonserm P. Crystal structure of BinB: A receptor binding component of the binary toxin from Lysinibacillus sphaericus. Proteins. 2014 Oct;82(10):2703-12. doi: 10.1002/prot.24636. Epub 2014 Jul 5. PMID:24975613 doi:http://dx.doi.org/10.1002/prot.24636
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