View source for 10pp


==Asymmetric architecture and adaptation of Treponema flagella==
<StructureSection load='10pp' size='340' side='right'caption='[[10pp]], [[Resolution|resolution]] 3.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[10pp]] is a 11 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=10PP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10PP 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]] 3.72&#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=10pp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10pp OCA], [https://pdbe.org/10pp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10pp RCSB], [https://www.ebi.ac.uk/pdbsum/10pp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10pp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q73MN3_TREDE Q73MN3_TREDE] Component of the core of the flagella.[ARBA:ARBA00004095][RuleBase:RU362073]
<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 10pp" 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]]