View source for 10pl


==Asymmetric architecture and adaptation of Treponema flagella==
<StructureSection load='10pl' size='340' side='right'caption='[[10pl]], [[Resolution|resolution]] 3.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[10pl]] is a 25 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola_ATCC_35405 Treponema denticola ATCC 35405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=10PL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10PL 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]] 3.44&#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=10pl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10pl OCA], [https://pdbe.org/10pl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10pl RCSB], [https://www.ebi.ac.uk/pdbsum/10pl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10pl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q73MU9_TREDE Q73MU9_TREDE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spirochetes exhibit a distinctive corkscrew-like motility driven by periplasmic flagella that wrap around the cell body in a supercoiled configuration, yet the structural basis of this propulsion remains poorly understood. Here we combine cryo-electron microscopy, cryo-electron tomography, and genetic and biochemical analyses to determine the assembly and adaptation principles of the supercoiled flagellar filament in Treponema denticola, a major periodontal pathogen. Near-atomic structures reveal a glycosylated FlaB flagellin core encased by an asymmetric sheath. The major sheath protein FlaA forms the bulk of the sheath and mechanically couples to the core through defined interfaces required for efficient motility, whereas four minor sheath proteins (FlaA1, FlaA2, FlaAP1, and FlaAP2) assemble along the concave side of the filament to accommodate intrinsic curvature. Disruption of this asymmetric core-sheath organization compromises force transmission and impairs motility, establishing coordinated asymmetric assembly as a fundamental mechanism underlying spirochetal motility.

Asymmetric architecture and adaptation of Treponema flagella.,Wang J, Kurniyati K, Guo W, Botting JM, Wu H, Sindelar CV, Li C, Liu J Nat Commun. 2026 Jun 19. doi: 10.1038/s41467-026-74267-7. PMID:42321199<ref>PMID:42321199</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 10pl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema denticola ATCC 35405]]
[[Category: Botting JM]]
[[Category: Guo W]]
[[Category: Kurniyati K]]
[[Category: Li C]]
[[Category: Liu J]]
[[Category: Sindelar CV]]
[[Category: Wang J]]