High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis
The Cyt family of proteins consists of δ-endotoxins expressed during sporulation of several subspecies of Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted mem...
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| Veröffentlicht in: | Journal of molecular biology 2008-07, Vol.380 (5), p.820-827 |
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| creator | Cohen, Shmuel Dym, Orly Albeck, Shira Ben-Dov, Eitan Cahan, Rivka Firer, Michael Zaritsky, Arieh |
| description | The Cyt family of proteins consists of δ-endotoxins expressed during sporulation of several subspecies of
Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted membrane destruction. The δ-endotoxins of subsp.
israelensis include three Cyt species: a major Cyt1Aa and two minor proteins, Cyt2Ba and Cyt1Ca. A cleaved Cyt protein that lacks the N- and C-terminal segments forms a toxic monomer. Here, we describe the crystal structure of Cyt2Ba, cleaved at its amino and carboxy termini by bacterial endogenous protease(s). Overall, its fold resembles that of the previously described volvatoxin A2 and the nontoxic form of Cyt2Aa. The structural similarity between these three proteins may provide information regarding the mechanism(s) of membrane-perforating toxins. |
| doi_str_mv | 10.1016/j.jmb.2008.05.010 |
| format | Article |
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Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted membrane destruction. The δ-endotoxins of subsp.
israelensis include three Cyt species: a major Cyt1Aa and two minor proteins, Cyt2Ba and Cyt1Ca. A cleaved Cyt protein that lacks the N- and C-terminal segments forms a toxic monomer. Here, we describe the crystal structure of Cyt2Ba, cleaved at its amino and carboxy termini by bacterial endogenous protease(s). Overall, its fold resembles that of the previously described volvatoxin A2 and the nontoxic form of Cyt2Aa. The structural similarity between these three proteins may provide information regarding the mechanism(s) of membrane-perforating toxins.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2008.05.010</identifier><identifier>PMID: 18571667</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>activated Cyt2Ba ; Amino Acid Sequence ; Bacillus thuringiensis ; Bacillus thuringiensis - classification ; Bacillus thuringiensis - genetics ; Bacillus thuringiensis - pathogenicity ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Conserved Sequence ; Crystallography, X-Ray ; Cyt toxins ; Endotoxins - chemistry ; Endotoxins - genetics ; Endotoxins - isolation & purification ; Endotoxins - metabolism ; Hemolysin Proteins - chemistry ; Hemolysin Proteins - genetics ; Hemolysin Proteins - isolation & purification ; Hemolysin Proteins - metabolism ; Hemolysis ; Humans ; Hydrolysis ; insecticidal crystal proteins ; membrane-active cytotoxin ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Pest Control, Biological ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; Solubility ; X-ray crystal structure</subject><ispartof>Journal of molecular biology, 2008-07, Vol.380 (5), p.820-827</ispartof><rights>2008 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c448t-88e262244359b07f2f8dc754661a28689818e85c9e25aa8a8da3a8aeb1d18f923</citedby><cites>FETCH-LOGICAL-c448t-88e262244359b07f2f8dc754661a28689818e85c9e25aa8a8da3a8aeb1d18f923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283608005639$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18571667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cohen, Shmuel</creatorcontrib><creatorcontrib>Dym, Orly</creatorcontrib><creatorcontrib>Albeck, Shira</creatorcontrib><creatorcontrib>Ben-Dov, Eitan</creatorcontrib><creatorcontrib>Cahan, Rivka</creatorcontrib><creatorcontrib>Firer, Michael</creatorcontrib><creatorcontrib>Zaritsky, Arieh</creatorcontrib><title>High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The Cyt family of proteins consists of δ-endotoxins expressed during sporulation of several subspecies of
Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted membrane destruction. The δ-endotoxins of subsp.
israelensis include three Cyt species: a major Cyt1Aa and two minor proteins, Cyt2Ba and Cyt1Ca. A cleaved Cyt protein that lacks the N- and C-terminal segments forms a toxic monomer. Here, we describe the crystal structure of Cyt2Ba, cleaved at its amino and carboxy termini by bacterial endogenous protease(s). Overall, its fold resembles that of the previously described volvatoxin A2 and the nontoxic form of Cyt2Aa. The structural similarity between these three proteins may provide information regarding the mechanism(s) of membrane-perforating toxins.</description><subject>activated Cyt2Ba</subject><subject>Amino Acid Sequence</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - classification</subject><subject>Bacillus thuringiensis - genetics</subject><subject>Bacillus thuringiensis - pathogenicity</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Conserved Sequence</subject><subject>Crystallography, X-Ray</subject><subject>Cyt toxins</subject><subject>Endotoxins - chemistry</subject><subject>Endotoxins - genetics</subject><subject>Endotoxins - isolation & purification</subject><subject>Endotoxins - metabolism</subject><subject>Hemolysin Proteins - chemistry</subject><subject>Hemolysin Proteins - genetics</subject><subject>Hemolysin Proteins - isolation & purification</subject><subject>Hemolysin Proteins - metabolism</subject><subject>Hemolysis</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>insecticidal crystal proteins</subject><subject>membrane-active cytotoxin</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Pest Control, Biological</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Solubility</subject><subject>X-ray crystal structure</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtr3DAUhUVJaaZpf0A2Qavu7Eqyrbkmq2RImkJKoY-1kOXrRINsTfQIzL-vkhnoLqsDl-8cuB8h55zVnHH5dVtv56EWjEHNuppx9o6sOIO-AtnACVkxJkQloJGn5GOMW8ZY17TwgZxy6NZcyvWKuDv78Fj9wuhdTtYvdBP2MWlHf6eQTcoBqZ_olUn2WScc6WafxLWmP_ziZwx0Cn6m19pY53Kk6TEHuzxYXKKNNOYh7mpqY9DoXk-fyPtJu4ifj3lG_t7e_NncVfc_v33fXN1Xpm0hVQAopBBt23T9wNaTmGA0666VkmsBEnrggNCZHkWnNWgYdVMCBz5ymHrRnJEvh91d8E8ZY1KzjQad0wv6HJUojjhnsoD8AJrgYww4qV2wsw57xZl6Uay2qihWL4oV61RRXDoXx_E8zDj-bxydFuDyAGB58dliUNEUJQZHG9AkNXr7xvw_FIaNUA</recordid><startdate>20080725</startdate><enddate>20080725</enddate><creator>Cohen, Shmuel</creator><creator>Dym, Orly</creator><creator>Albeck, Shira</creator><creator>Ben-Dov, Eitan</creator><creator>Cahan, Rivka</creator><creator>Firer, Michael</creator><creator>Zaritsky, Arieh</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20080725</creationdate><title>High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis</title><author>Cohen, Shmuel ; Dym, Orly ; Albeck, Shira ; Ben-Dov, Eitan ; Cahan, Rivka ; Firer, Michael ; Zaritsky, Arieh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c448t-88e262244359b07f2f8dc754661a28689818e85c9e25aa8a8da3a8aeb1d18f923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>activated Cyt2Ba</topic><topic>Amino Acid Sequence</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - classification</topic><topic>Bacillus thuringiensis - genetics</topic><topic>Bacillus thuringiensis - pathogenicity</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Conserved Sequence</topic><topic>Crystallography, X-Ray</topic><topic>Cyt toxins</topic><topic>Endotoxins - chemistry</topic><topic>Endotoxins - genetics</topic><topic>Endotoxins - isolation & purification</topic><topic>Endotoxins - metabolism</topic><topic>Hemolysin Proteins - chemistry</topic><topic>Hemolysin Proteins - genetics</topic><topic>Hemolysin Proteins - isolation & purification</topic><topic>Hemolysin Proteins - metabolism</topic><topic>Hemolysis</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>insecticidal crystal proteins</topic><topic>membrane-active cytotoxin</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Pest Control, Biological</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solubility</topic><topic>X-ray crystal structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cohen, Shmuel</creatorcontrib><creatorcontrib>Dym, Orly</creatorcontrib><creatorcontrib>Albeck, Shira</creatorcontrib><creatorcontrib>Ben-Dov, Eitan</creatorcontrib><creatorcontrib>Cahan, Rivka</creatorcontrib><creatorcontrib>Firer, Michael</creatorcontrib><creatorcontrib>Zaritsky, Arieh</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cohen, Shmuel</au><au>Dym, Orly</au><au>Albeck, Shira</au><au>Ben-Dov, Eitan</au><au>Cahan, Rivka</au><au>Firer, Michael</au><au>Zaritsky, Arieh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2008-07-25</date><risdate>2008</risdate><volume>380</volume><issue>5</issue><spage>820</spage><epage>827</epage><pages>820-827</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The Cyt family of proteins consists of δ-endotoxins expressed during sporulation of several subspecies of
Bacillus thuringiensis. Its members possess insecticidal, hemolytic, and cytolytic activities through pore formation and attract attention due to their potential use as vehicles for targeted membrane destruction. The δ-endotoxins of subsp.
israelensis include three Cyt species: a major Cyt1Aa and two minor proteins, Cyt2Ba and Cyt1Ca. A cleaved Cyt protein that lacks the N- and C-terminal segments forms a toxic monomer. Here, we describe the crystal structure of Cyt2Ba, cleaved at its amino and carboxy termini by bacterial endogenous protease(s). Overall, its fold resembles that of the previously described volvatoxin A2 and the nontoxic form of Cyt2Aa. The structural similarity between these three proteins may provide information regarding the mechanism(s) of membrane-perforating toxins.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>18571667</pmid><doi>10.1016/j.jmb.2008.05.010</doi><tpages>8</tpages></addata></record> |
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| subjects | activated Cyt2Ba Amino Acid Sequence Bacillus thuringiensis Bacillus thuringiensis - classification Bacillus thuringiensis - genetics Bacillus thuringiensis - pathogenicity Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Conserved Sequence Crystallography, X-Ray Cyt toxins Endotoxins - chemistry Endotoxins - genetics Endotoxins - isolation & purification Endotoxins - metabolism Hemolysin Proteins - chemistry Hemolysin Proteins - genetics Hemolysin Proteins - isolation & purification Hemolysin Proteins - metabolism Hemolysis Humans Hydrolysis insecticidal crystal proteins membrane-active cytotoxin Models, Molecular Molecular Sequence Data Molecular Weight Pest Control, Biological Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Homology, Amino Acid Solubility X-ray crystal structure |
| title | High-Resolution Crystal Structure of Activated Cyt2Ba Monomer from Bacillus thuringiensis subsp. israelensis |
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