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| | <StructureSection load='6xky' size='340' side='right'caption='[[6xky]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='6xky' size='340' side='right'caption='[[6xky]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6xky]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Cauvn Cauvn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XKY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xky]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_NA1000 Caulobacter vibrioides NA1000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XKY FirstGlance]. <br> |
| - | </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=6xky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xky OCA], [https://pdbe.org/6xky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xky RCSB], [https://www.ebi.ac.uk/pdbsum/6xky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xky ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</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=6xky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xky OCA], [https://pdbe.org/6xky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xky RCSB], [https://www.ebi.ac.uk/pdbsum/6xky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xky ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/A0A0H3C7K6_CAUVN A0A0H3C7K6_CAUVN]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073]
| + | [https://www.uniprot.org/uniprot/FLJK_CAUVC FLJK_CAUVC] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Caulobacter crescentus is a Gram-negative alpha-proteobacterium that commonly lives in oligotrophic fresh and salt-water environments. C. crescentus is a host to many bacteriophages, including varphiCbK and varphiCbK-like bacteriophages, which require interaction with the bacterial flagellum and pilus complexes during adsorption. It is commonly thought that the six paralogs of the flagellin gene present in C. crescentus are important for bacteriophage evasion. Here, we show that deletion of specific flagellins in C. crescentus can indeed attenuate varphiCbK adsorption efficiency, although no single deletion completely ablates varphiCbK adsorption. Thus, bacteriophage varphiCbK likely recognizes a common motif among the six known flagellins in C. crescentus with varying degrees of efficiency. Interestingly, we observe that most deletion strains still generate flagellar filaments, with the exception of a strain that contains only the most divergent flagellin, FljJ, or a strain that contains only FljN and FljO. To visualize the surface residues that are likely recognized by varphiCbK, we determined two high-resolution structures of the FljK filament, with and without an amino acid substitution that induces straightening of the filament. We observe post-translational modifications on conserved, surface threonine residues of FljK that are likely O-linked glycans. The possibility of interplay between these modifications and varphiCbK adsorption is discussed. We also determined the structure of a filament composed of a heterogeneous mixture of FljK and FljL, the final resolution of which was limited to approximately 4.6 A. Altogether, this work builds a platform for future investigations of how phage varphiCbK infects C. crescentus at the molecular level.IMPORTANCE Bacterial flagellar filaments serve as an initial attachment point for many bacteriophages to bacteria. Some bacteria harbor numerous flagellin genes, and are therefore able to generate flagellar filaments with complex compositions, which is thought to be important for evasion from bacteriophages. This study characterizes the importance of the six flagellin genes in C. crescentus for infection by bacteriophage varphiCbK. We find that filaments containing the FljK flagellin are the preferred substrate for bacteriophage varphiCbK. We also present a high-resolution structure of a flagellar filament containing only the FljK flagellin, which provides a platform for future studies on determining how bacteriophage varphiCbK attaches to flagellar filaments at the molecular level.
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| - | Flagellar Structures from the Bacterium Caulobacter crescentus and Implications for Phage PhiCbK Predation of Multi-Flagellin Bacteria.,Montemayor EJ, Ploscariu NT, Sanchez JC, Parrell D, Dillard RS, Shebelut CW, Ke Z, Guerrero-Ferreira RC, Wright ER J Bacteriol. 2020 Dec 7. pii: JB.00399-20. doi: 10.1128/JB.00399-20. PMID:33288623<ref>PMID:33288623</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 6xky" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Flagellin 3D structures|Flagellin 3D structures]] | | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cauvn]] | + | [[Category: Caulobacter vibrioides NA1000]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dillard, R S]] | + | [[Category: Dillard RS]] |
| - | [[Category: Guerrero-Ferreira, R C]] | + | [[Category: Guerrero-Ferreira RC]] |
| - | [[Category: Ke, Z]] | + | [[Category: Ke Z]] |
| - | [[Category: Montemayor, E J]] | + | [[Category: Montemayor EJ]] |
| - | [[Category: Parrell, D]] | + | [[Category: Parrell D]] |
| - | [[Category: Ploscariu, N T]] | + | [[Category: Ploscariu NT]] |
| - | [[Category: Sanchez, J C]] | + | [[Category: Sanchez JC]] |
| - | [[Category: Shebelut, C W]] | + | [[Category: Shebelut CW]] |
| - | [[Category: Wright, E R]] | + | [[Category: Wright ER]] |
| - | [[Category: Caulobacter]]
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| - | [[Category: Filament]]
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| - | [[Category: Flagellin]]
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| - | [[Category: Flagellum]]
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| - | [[Category: Helical]]
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| - | [[Category: Motility]]
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| - | [[Category: Structural protein]]
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