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6kty

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<StructureSection load='6kty' size='340' side='right'caption='[[6kty]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='6kty' size='340' side='right'caption='[[6kty]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kty]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KTY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kty]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KTY FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kty OCA], [http://pdbe.org/6kty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kty RCSB], [http://www.ebi.ac.uk/pdbsum/6kty PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kty ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kty OCA], [https://pdbe.org/6kty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kty RCSB], [https://www.ebi.ac.uk/pdbsum/6kty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kty ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q6MQ71_BDEBA Q6MQ71_BDEBA]] Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.[RuleBase:RU362066]
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[https://www.uniprot.org/uniprot/Q6MQ71_BDEBA Q6MQ71_BDEBA] Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.[RuleBase:RU362066]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bdellovibrio bacteriovorus is a predator bacterial species of the Deltaproteobacteria class that requires flagellum-mediated motility to initiate the parasitization of other gram-negative bacteria. The flagellum is capped by FliD, which polymerizes flagellin into a flagellar filament. FliD has been reported to function as a species-specific oligomer, such as a tetramer, a pentamer, or a hexamer, in members of the Gammaproteobacteria class. However, the oligomeric state and structural features of FliD from bacterial species outside the Gammaproteobacteria class are unknown. Based on structural and biochemical analyses, we report here that B. bacteriovorus FliD (bbFliD) forms a tetramer. bbFliD tetramerizes in a circular head-to-tail arrangement by inserting the D2 domain of one subunit into the concave surface of the second subunit generated between the D2 and D3 domains as observed in Serratia marcescens FliD. However, bbFliD adopts a more compact and flat oligomeric structure, which exhibits a more extended tetramerization interface flanked by two additional surfaces due to different intersubunit and interdomain organizations as well as an elongated loop. In conclusion, FliD from B. bacteriovorus, which belongs to the Deltaproteobacteria class, also produces a tetramer similar to FliD from Gammaproteobacterial species but adopts a unique species-specific oligomeric structure.
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Crystal structure of the flagellar cap protein FliD from Bdellovibrio bacteriovorus.,Cho SY, Song WS, Yoon SI Biochem Biophys Res Commun. 2019 Nov 12;519(3):652-658. doi:, 10.1016/j.bbrc.2019.09.024. Epub 2019 Sep 18. PMID:31542231<ref>PMID:31542231</ref>
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==See Also==
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*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kty" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bdellovibrio bacteriovorus HD100]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cho, S Y]]
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[[Category: Cho SY]]
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[[Category: Yoon, S I]]
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[[Category: Yoon SI]]
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[[Category: Bacterial flagellar cap protein]]
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[[Category: Structural protein]]
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Current revision

Crystal structure of the flagellar cap protein FliD from Bdellovibrio bacteriovorus

PDB ID 6kty

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