4ary: Difference between revisions
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<StructureSection load='4ary' size='340' side='right'caption='[[4ary]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='4ary' size='340' side='right'caption='[[4ary]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ary]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ary]] 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=4ARY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARY FirstGlance]. <br> | ||
</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=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | </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=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4arx|4arx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4arx|4arx]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ary FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ary OCA], [https://pdbe.org/4ary PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ary RCSB], [https://www.ebi.ac.uk/pdbsum/4ary PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ary ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CR1AC_BACTK CR1AC_BACTK]] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:44, 25 August 2022
Lepidopteran-specific toxin Cry1Ac in complex with receptor specificity determinant GalNAcLepidopteran-specific toxin Cry1Ac in complex with receptor specificity determinant GalNAc
Structural highlights
Function[CR1AC_BACTK] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae. Publication Abstract from PubMedCry1Ac 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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