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< | ==Crystal Structure of Insecticidal Delta-Endotoxin Cry8Ea1 from Bacillus Thuringiensis at 2.2 Angstroms Resolution== | ||
<StructureSection load='3eb7' size='340' side='right'caption='[[3eb7]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3eb7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2qkg 2qkg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EB7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3eb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eb7 OCA], [https://pdbe.org/3eb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eb7 RCSB], [https://www.ebi.ac.uk/pdbsum/3eb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eb7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3LEP7_BACTU B3LEP7_BACTU] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/3eb7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3eb7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystal (Cry) proteins belong to an insect toxin family encoded and expressed by a variety of Bacillus thuringiensis isolates, and are named due to their in vivo auto-crystallization abilities. To kill the infected host insects, protease-activated Cry toxins should firstly be recognized by certain membrane receptors on the surface of insect midgut epithelial cells and consequently assemble together as lethal transmembrane pores. Here we report the 2.2-A crystal structure of Cry8Ea1 toxin, a Cry family member specifically toxic to the underground larvae of Holotrichia parallela. Superimposition of the domain I from Cry8Ea1 and other structurally characterized Cry toxins reveals an identical surface proline residue and a highly conserved kink of a helix, both of which have drawn comparatively little attention from previous researchers. Further structural analysis and functional studies suggest that both the proline and the helix kink might be essential in exposing a helix-helix hairpin, which is believed to be the very first step in the well-known "umbrella" model of the membrane penetration. In summary, we propose a plausible model of the initiation of Cry toxin domain I disassembly before membrane penetration and pore formation. | |||
Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela.,Guo S, Ye S, Liu Y, Wei L, Xue J, Wu H, Song F, Zhang J, Wu X, Huang D, Rao Z J Struct Biol. 2009 Nov;168(2):259-66. Epub 2009 Jul 8. PMID:19591941<ref>PMID:19591941</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3eb7" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Delta-endotoxin|Delta-endotoxin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus thuringiensis]] | [[Category: Bacillus thuringiensis]] | ||
[[Category: Guo | [[Category: Large Structures]] | ||
[[Category: Shu | [[Category: Guo S]] | ||
[[Category: Song | [[Category: Shu CL]] | ||
[[Category: Wei | [[Category: Song F]] | ||
[[Category: Ye | [[Category: Wei L]] | ||
[[Category: Zhang | [[Category: Ye S]] | ||
[[Category: Zhang J]] | |||
Latest revision as of 18:20, 1 November 2023
Crystal Structure of Insecticidal Delta-Endotoxin Cry8Ea1 from Bacillus Thuringiensis at 2.2 Angstroms ResolutionCrystal Structure of Insecticidal Delta-Endotoxin Cry8Ea1 from Bacillus Thuringiensis at 2.2 Angstroms Resolution
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal (Cry) proteins belong to an insect toxin family encoded and expressed by a variety of Bacillus thuringiensis isolates, and are named due to their in vivo auto-crystallization abilities. To kill the infected host insects, protease-activated Cry toxins should firstly be recognized by certain membrane receptors on the surface of insect midgut epithelial cells and consequently assemble together as lethal transmembrane pores. Here we report the 2.2-A crystal structure of Cry8Ea1 toxin, a Cry family member specifically toxic to the underground larvae of Holotrichia parallela. Superimposition of the domain I from Cry8Ea1 and other structurally characterized Cry toxins reveals an identical surface proline residue and a highly conserved kink of a helix, both of which have drawn comparatively little attention from previous researchers. Further structural analysis and functional studies suggest that both the proline and the helix kink might be essential in exposing a helix-helix hairpin, which is believed to be the very first step in the well-known "umbrella" model of the membrane penetration. In summary, we propose a plausible model of the initiation of Cry toxin domain I disassembly before membrane penetration and pore formation. Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela.,Guo S, Ye S, Liu Y, Wei L, Xue J, Wu H, Song F, Zhang J, Wu X, Huang D, Rao Z J Struct Biol. 2009 Nov;168(2):259-66. Epub 2009 Jul 8. PMID:19591941[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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