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| | {{STRUCTURE_1w99| PDB=1w99 | SCENE= }} | | {{STRUCTURE_1w99| PDB=1w99 | SCENE= }} |
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| - | '''MOSQUITO-LARVICIDAL TOXIN CRY4BA FROM BACILLUS THURINGIENSIS SSP. ISRAELENSIS'''
| + | ===MOSQUITO-LARVICIDAL TOXIN CRY4BA FROM BACILLUS THURINGIENSIS SSP. ISRAELENSIS=== |
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| - | ==Overview==
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| - | Cry4Ba, isolated from Bacillus thuringiensis subsp. israelensis, is specifically toxic to the larvae of Aedes and Anopheles mosquitoes. The structure of activated Cry4Ba toxin has been determined by multiple isomorphous replacement with anomalous scattering and refined to R(cryst) = 20.5% and R(free)= 21.8% at 1.75 Angstroms resolution. It resembles previously reported Cry toxin structures but shows the following distinctions. In domain I the helix bundle contains only the long and amphipathic helices alpha3-alpha7. The N-terminal helices alpha1-alpha2b, absent due to proteolysis during crystallisation, appear inessential to toxicity. In domain II the beta-sheet prism presents short apical loops without the beta-ribbon extension of inner strands, thus placing the receptor combining sites close to the sheets. In domain III the beta-sandwich contains a helical extension from the C-terminal strand beta23, which interacts with a beta-hairpin excursion from the edge of the outer sheet. The structure provides a rational explanation of recent mutagenesis and biophysical data on this toxin. Furthermore, added to earlier structures from the Cry toxin family, Cry4Ba completes a minimal structural database covering the Coleoptera, Lepidoptera, Diptera and Lepidoptera/Diptera specificity classes. A multiple structure alignment found that the Diptera-specific Cry4Ba is structurally more closely similar to the Lepidoptera-specific Cry1Aa than the Coleoptera-specific Cry3Aa, but most distantly related to Lepidoptera/Diptera-specific Cry2Aa. The structures are most divergent in domain II, supporting the suggestion that this domain has a major role in specificity determination. They are most similar in the alpha3-alpha7 major fragment of domain I, which contains the alpha4-alpha5 hairpin crucial to pore formation. The collective knowledge of Cry toxin structure and mutagenesis data will lead to a more critical understanding of the structural basis for receptor binding and pore formation, as well as allowing the scope of diversity to be better appreciated.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15811374}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15811374 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15811374}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Membrane pore]] | | [[Category: Membrane pore]] |
| | [[Category: Toxin]] | | [[Category: Toxin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:20:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:55:28 2008'' |
Revision as of 06:55, 29 July 2008
Template:STRUCTURE 1w99
MOSQUITO-LARVICIDAL TOXIN CRY4BA FROM BACILLUS THURINGIENSIS SSP. ISRAELENSIS
Template:ABSTRACT PUBMED 15811374
About this Structure
1W99 is a Single protein structure of sequence from Bacillus thuringiensis serovar israelensis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications., Boonserm P, Davis P, Ellar DJ, Li J, J Mol Biol. 2005 Apr 29;348(2):363-82. PMID:15811374
Page seeded by OCA on Tue Jul 29 09:55:28 2008
