8jmv
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8jmv is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Flagellar fibrils from Bacillus amyloliquefaciens== | |
| + | <StructureSection load='8jmv' size='340' side='right'caption='[[8jmv]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8jmv]] is a 33 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JMV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</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=8jmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jmv OCA], [https://pdbe.org/8jmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jmv RCSB], [https://www.ebi.ac.uk/pdbsum/8jmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jmv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria develop a variety of extracellular fibrous structures crucial for their survival, such as flagella and pili. In this study, we use cryo-EM to identify protein fibrils surrounding lab-cultured Bacillus amyloiquefaciens and discover an unreported fibril species in addition to the flagellar fibrils. These previously unknown fibrils are composed of Vpr, an extracellular serine peptidase. We find that Vpr assembles into fibrils in an enzymatically active form, potentially representing a strategy of enriching Vpr activities around bacterial cells. Vpr fibrils are also observed under other culture conditions and around other Bacillus bacteria, such as Bacillus subtilis, which may suggest a general mechanism across all Bacillus bacterial groups. Taken together, our study reveals fibrils outside the bacterial cell and sheds light on the physiological role of these extracellular fibrils. | ||
| - | + | Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM.,Cheng Y, Han J, Song M, Zhang S, Cao Q Nat Commun. 2023 Nov 18;14(1):7503. doi: 10.1038/s41467-023-43359-z. PMID:37980359<ref>PMID:37980359</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8jmv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus amyloliquefaciens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cao Q]] | ||
| + | [[Category: Cheng Y]] | ||
Current revision
Flagellar fibrils from Bacillus amyloliquefaciens
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