9n0b

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'''Unreleased structure'''
 
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The entry 9n0b is ON HOLD
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==Cryo-EM of spore appendage from Anaerovoracaceae==
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<StructureSection load='9n0b' size='340' side='right'caption='[[9n0b]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9n0b]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillota_bacterium Bacillota bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9N0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9N0B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9n0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9n0b OCA], [https://pdbe.org/9n0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9n0b RCSB], [https://www.ebi.ac.uk/pdbsum/9n0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9n0b ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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For over 100 years, Bacillus thuringiensis (Bt) has been used as an agricultural biopesticide to control pests caused by insect species in the orders of Lepidoptera, Diptera, and Coleoptera. Under nutrient starvation, Bt cells differentiate into spores and associated toxin crystals that can adopt biofilm-like aggregates. We reveal that such Bt spore/toxin biofilms are embedded in a fibrous extrasporal matrix, and using cryoID, we resolved the structure and molecular identity of an uncharacterized type of pili, referred to here as Fibrillar ENdospore Appendages or F-ENA. F-ENA are monomolecular protein filaments anchored to the exosporium and tipped with a flexible fibrillum. Phylogenetic and structural analyses reveal that F-ENA are conserved in Bacilli and Clostridia, featuring head-neck domains with beta-barrel necks that interlock via N-terminal hook peptides. In Bacillus, two collagen-like proteins (F-Anchor and F-BclA), respectively, tether F-ENA and form the distal tip. Sedimentation assays suggest F-ENA promotes spore clustering via F-BclA contacts and/or filament bundling.
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Authors:
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Cryo-EM identifies F-ENA of Bacillus thuringiensis as a widespread family of endospore appendages across Firmicutes.,Sleutel M, Sogues A, Van Gerven N, Jonsmoen UL, Van Molle I, Fislage M, Theunissen LD, Bellis NF, Baquero DP, Egelman EH, Krupovic M, Wang F, Aspholm M, Remaut H Nat Commun. 2025 Aug 16;16(1):7652. doi: 10.1038/s41467-025-62896-3. PMID:40818982<ref>PMID:40818982</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9n0b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillota bacterium]]
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[[Category: Large Structures]]
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[[Category: Baquero DP]]
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[[Category: Bellis NF]]
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[[Category: Egelman EH]]
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[[Category: Krupovic M]]
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[[Category: Wang F]]

Current revision

Cryo-EM of spore appendage from Anaerovoracaceae

PDB ID 9n0b

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