View source for 9atb


==cryo-EM of Cupriavidus gilardii flagellum==
<StructureSection load='9atb' size='340' side='right'caption='[[9atb]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9atb]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_gilardii Cupriavidus gilardii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ATB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ATB 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=9atb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9atb OCA], [https://pdbe.org/9atb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9atb RCSB], [https://www.ebi.ac.uk/pdbsum/9atb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9atb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A849B394_9BURK A0A849B394_9BURK] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Supercoiled flagellar filaments function as mechanical propellers within the bacterial flagellum complex, playing a crucial role in motility. Flagellin, the building block of the filament, features a conserved inner D0/D1 core domain across different bacterial species. In contrast, approximately half of the flagellins possess additional, highly divergent outer domain(s), suggesting varied functional potential. In this study, we report atomic structures of flagellar filaments from three distinct bacterial species: Cupriavidus gilardii, Stenotrophomonas maltophilia, and Geovibrio thiophilus. Our findings reveal that the flagella from the facultative anaerobic G. thiophilus possesses a significantly more negatively charged surface, potentially enabling adhesion to positively charged minerals. Furthermore, we analyze all AlphaFold predicted structures for annotated bacterial flagellins, categorizing the flagellin outer domains into 682 structural clusters. This classification provides insights into the prevalence and experimental verification of these outer domains. Remarkably, two of the flagellar structures reported herein belong to a distinct cluster, indicating additional opportunities on the study of the functional diversity of flagellar outer domains. Our findings underscore the complexity of bacterial flagellins and open up possibilities for future studies into their varied roles beyond motility.

Structural diversity and clustering of bacterial flagellar outer domains.,Fields JL, Zhang H, Bellis NF, Petersen HA, Halder SK, Rich-New ST, Krupovic M, Wu H, Wang F Nat Commun. 2024 Nov 3;15(1):9500. doi: 10.1038/s41467-024-53923-w. PMID:39489766<ref>PMID:39489766</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9atb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cupriavidus gilardii]]
[[Category: Large Structures]]
[[Category: Fields JL]]
[[Category: Halder SK]]
[[Category: Wang F]]
[[Category: Wu H]]
[[Category: Zhang H]]