4yn1: Difference between revisions
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<StructureSection load='4yn1' size='340' side='right'caption='[[4yn1]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4yn1' size='340' side='right'caption='[[4yn1]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yn1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4yn1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anomala_cuprea_entomopoxvirus Anomala cuprea entomopoxvirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YN1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4yn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yn1 OCA], [https://pdbe.org/4yn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yn1 RCSB], [https://www.ebi.ac.uk/pdbsum/4yn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yn1 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O70709_9POXV O70709_9POXV] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Anomala cuprea entomopoxvirus]] | [[Category: Anomala cuprea entomopoxvirus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bunker | [[Category: Bunker RD]] | ||
[[Category: Chiu | [[Category: Chiu E]] | ||
[[Category: Metcalf | [[Category: Metcalf P]] | ||
Revision as of 11:20, 3 May 2023
THE ATOMIC STRUCTURE OF ANOMALA CUPREA ENTOMOPOXVIRUS (ACEPV) FUSOLIN SPINDLESTHE ATOMIC STRUCTURE OF ANOMALA CUPREA ENTOMOPOXVIRUS (ACEPV) FUSOLIN SPINDLES
Structural highlights
FunctionPublication Abstract from PubMedThe great benefits that chemical pesticides have brought to agriculture are partly offset by widespread environmental damage to nontarget species and threats to human health. Microbial bioinsecticides are considered safe and highly specific alternatives but generally lack potency. Spindles produced by insect poxviruses are crystals of the fusolin protein that considerably boost not only the virulence of these viruses but also, in cofeeding experiments, the insecticidal activity of unrelated pathogens. However, the mechanisms by which spindles assemble into ultra-stable crystals and enhance virulence are unknown. Here we describe the structure of viral spindles determined by X-ray microcrystallography from in vivo crystals purified from infected insects. We found that a C-terminal molecular arm of fusolin mediates the assembly of a globular domain, which has the hallmarks of lytic polysaccharide monooxygenases of chitinovorous bacteria. Explaining their unique stability, a 3D network of disulfide bonds between fusolin dimers covalently crosslinks the entire crystalline matrix of spindles. However, upon ingestion by a new host, removal of the molecular arm abolishes this stabilizing network leading to the dissolution of spindles. The released monooxygenase domain is then free to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. The mode of action revealed here may guide the design of potent spindles as synergetic additives to bioinsecticides. Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization.,Chiu E, Hijnen M, Bunker RD, Boudes M, Rajendran C, Aizel K, Olieric V, Schulze-Briese C, Mitsuhashi W, Young V, Ward VK, Bergoin M, Metcalf P, Coulibaly F Proc Natl Acad Sci U S A. 2015 Mar 18. pii: 201418798. PMID:25787255[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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