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3ron

From Proteopedia

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Current revision (12:31, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3ron' size='340' side='right'caption='[[3ron]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
<StructureSection load='3ron' size='340' side='right'caption='[[3ron]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ron]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacti Bacti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RON FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ron]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis Bacillus thuringiensis serovar israelensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RON FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyt1Aa, cytA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1430 BACTI])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</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=3ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ron OCA], [https://pdbe.org/3ron PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ron RCSB], [https://www.ebi.ac.uk/pdbsum/3ron PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ron 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=3ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ron OCA], [https://pdbe.org/3ron PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ron RCSB], [https://www.ebi.ac.uk/pdbsum/3ron PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ron ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CT1AA_BACTI CT1AA_BACTI]] Kills the larvae of dipteran insects by making pores in the epithelial cell membrane of the insect midgut. Acts on mosquitos and black flies.
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[https://www.uniprot.org/uniprot/CT1AA_BACTI CT1AA_BACTI] Kills the larvae of dipteran insects by making pores in the epithelial cell membrane of the insect midgut. Acts on mosquitos and black flies.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During sporulation, Bacillus thuringiensis subsp. israelensis produces a mosquito larvicidal protein complex containing several crystalline and cytolytic (Cyt) toxins. Here, the activated monomeric form of Cyt1Aa, the most toxic Cyt family member, was isolated and crystallized, and its structure was determined for the first time at 2.2 A resolution. Cyt1Aa adopts a typical cytolysin fold containing a beta-sheet held by two surrounding alpha-helical layers. The absence of a beta-strand (between residues V26 and I37) in the dimeric structure of Cyt2Aa led us to deduce that this is the only essential segment for dimer formation and that activation of the toxin occurs by proteolytic processing of its N-terminus. Based on the Cyt1Aa structure, we suggest that the toxicity of Cyt1Aa and other nonrelated proteins, all sharing a cytolysin fold, is correlated with their ability to undergo conformational changes that are necessary prior to their membrane insertion and perforation. This fold allows the alpha-helical layers to swing away, exposing the beta-sheet to insert into the membrane. The identification of a putative lipid binding pocket between the beta-sheet and the helical layer of Cyt1Aa supports this mechanism. Sequence-based structural analysis of Cyt1Aa revealed that the lack of activity of Cyt1Ca may be related to the latter's inability to undergo this conformational change due to its lack of flexibility. The pattern of the hemolytic activity of Cyt1Aa presented here (resembling that of pore-forming agents), while differing from that imposed by ionic and nonionic detergents, further supports the pore-forming model by which conformational changes occur prior to membrane insertion and perforation.
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Cyt1Aa Toxin: High-Resolution Structure Reveals Implications for Its Membrane-Perforating Function.,Cohen S, Albeck S, Ben-Dov E, Cahan R, Firer M, Zaritsky A, Dym O J Mol Biol. 2011 Sep 19. PMID:21959261<ref>PMID:21959261</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ron" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Delta-endotoxin|Delta-endotoxin]]
*[[Delta-endotoxin|Delta-endotoxin]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacti]]
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[[Category: Bacillus thuringiensis serovar israelensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Albeck, S]]
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[[Category: Albeck S]]
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[[Category: Ben-Dov, E]]
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[[Category: Ben-Dov E]]
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[[Category: Cahan, R]]
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[[Category: Cahan R]]
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[[Category: Cohen, S]]
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[[Category: Cohen S]]
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[[Category: Dym, O]]
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[[Category: Dym O]]
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[[Category: Firer, M]]
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[[Category: Firer M]]
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[[Category: ISPC, Israel Structural Proteomics Center]]
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[[Category: Zaritsky A]]
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[[Category: Zaritsky, A]]
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[[Category: Cell invasion]]
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[[Category: Cytolysin fold]]
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[[Category: Structural genomic]]
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Current revision

Crystal Structure and Hemolytic Activity of the Cyt1Aa Toxin from Bacillus thuringiensis subsp. israelensis

PDB ID 3ron

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