8cwm: Difference between revisions

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'''Unreleased structure'''


The entry 8cwm is ON HOLD
==Cryo-EM structure of the supercoiled S. islandicus REY15A archaeal flagellar filament==
<StructureSection load='8cwm' size='340' side='right'caption='[[8cwm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cwm]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus_REY15A Sulfolobus islandicus REY15A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CWM 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]] 3.4&#8491;</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=8cwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cwm OCA], [https://pdbe.org/8cwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cwm RCSB], [https://www.ebi.ac.uk/pdbsum/8cwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cwm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0NG73_SULIR F0NG73_SULIR] Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.[RuleBase:RU361282]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The supercoiling of bacterial and archaeal flagellar filaments is required for motility. Archaeal flagellar filaments have no homology to their bacterial counterparts and are instead homologs of bacterial type IV pili. How these prokaryotic flagellar filaments, each composed of thousands of copies of identical subunits, can form stable supercoils under torsional stress is a fascinating puzzle for which structural insights have been elusive. Advances in cryoelectron microscopy (cryo-EM) make it now possible to directly visualize the basis for supercoiling, and here, we show the atomic structures of supercoiled bacterial and archaeal flagellar filaments. For the bacterial flagellar filament, we identify 11 distinct protofilament conformations with three broad classes of inter-protomer interface. For the archaeal flagellar filament, 10 protofilaments form a supercoil geometry supported by 10 distinct conformations, with one inter-protomer discontinuity creating a seam inside of the curve. Our results suggest that convergent evolution has yielded stable superhelical geometries that enable microbial locomotion.


Authors:  
Convergent evolution in the supercoiling of prokaryotic flagellar filaments.,Kreutzberger MAB, Sonani RR, Liu J, Chatterjee S, Wang F, Sebastian AL, Biswas P, Ewing C, Zheng W, Poly F, Frankel G, Luisi BF, Calladine CR, Krupovic M, Scharf BE, Egelman EH Cell. 2022 Sep 15;185(19):3487-3500.e14. doi: 10.1016/j.cell.2022.08.009. Epub , 2022 Sep 2. PMID:36057255<ref>PMID:36057255</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8cwm" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Flagellin 3D structures|Flagellin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus islandicus REY15A]]
[[Category: Egelman EH]]
[[Category: Kreutzberger MAB]]
[[Category: Krupovic M]]
[[Category: Liu J]]

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