4arx

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4arx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_kurstaki Bacillus thuringiensis serovar kurstaki]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARX FirstGlance]. <br>
<table><tr><td colspan='2'>[[4arx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_kurstaki Bacillus thuringiensis serovar kurstaki]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13D:1,3-DIAMINOPROPANE'>13D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ary|4ary]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13D:1,3-DIAMINOPROPANE'>13D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4arx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arx OCA], [https://pdbe.org/4arx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arx RCSB], [https://www.ebi.ac.uk/pdbsum/4arx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arx 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=4arx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arx OCA], [https://pdbe.org/4arx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arx RCSB], [https://www.ebi.ac.uk/pdbsum/4arx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CR1AC_BACTK CR1AC_BACTK]] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.
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[https://www.uniprot.org/uniprot/CR1AC_BACTK CR1AC_BACTK] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cry1Ac from Bacillus thuringiensis ssp. kurstaki HD-73 is a pore-forming protein specifically toxic to lepidopteran insect larvae. It binds to the cell-surface receptor aminopeptidase N in Manduca sexta midgut via the sugar N-acetyl-D-galactosamine (GalNAc). By using 1,3-diaminopropane (DAP) as the buffer throughout protoxin activation and chromatography on Q-Sepharose at pH 10.3, trypsin-activated Cry1Ac has been purified in a monomeric state, which was crucial to obtaining single crystals of Cry1Ac and of the Cry1Ac-GalNAc complex. Crystals of Cry1Ac alone are triclinic, with unit-cell parameters a = 51.78, b = 113.23, c = 123.41 A, alpha = 113.11, beta = 91.49, gamma = 100.46 degrees; those of the Cry1Ac-GalNAc complex show P2(1) symmetry, with unit-cell parameters a = 121.36, b = 51.19, c = 210.56 A, beta = 105.75 degrees. Data sets collected to 2.36 and 2.95 A resolution, respectively, show that both crystal forms contain four molecules of the 66 kDa toxin in the asymmetric unit and have related packing arrangements. The deaggregating effect of DAP may be explained by its capacity for bivalent hydrogen bonding and hydrophobic interactions at protein interfaces.
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Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine.,Derbyshire DJ, Ellar DJ, Li J Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1938-44. Epub 2001 Nov, 21. PMID:11717524<ref>PMID:11717524</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 4arx" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Delta-endotoxin|Delta-endotoxin]]
*[[Delta-endotoxin|Delta-endotoxin]]
*[[Pesticidal crystal protein|Pesticidal crystal protein]]
*[[Pesticidal crystal protein|Pesticidal crystal protein]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus thuringiensis serovar kurstaki]]
[[Category: Bacillus thuringiensis serovar kurstaki]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Carroll, J]]
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[[Category: Carroll J]]
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[[Category: Derbyshire, D J]]
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[[Category: Derbyshire DJ]]
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[[Category: Ellar, D J]]
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[[Category: Ellar DJ]]
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[[Category: Li, J]]
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[[Category: Li J]]
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[[Category: Insecticidal protein lepidopteran specificity]]
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[[Category: Membrane pore-forming toxin]]
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[[Category: Receptor binding site]]
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[[Category: Toxin]]
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Current revision

Lepidoptera-specific toxin Cry1Ac from Bacillus thuringiensis ssp. kurstaki HD-73

PDB ID 4arx

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