6gow: Difference between revisions
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The | ==Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121== | ||
<StructureSection load='6gow' size='340' side='right' caption='[[6gow]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gow]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GOW FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5maw|5maw]]</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=6gow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gow OCA], [http://pdbe.org/6gow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gow RCSB], [http://www.ebi.ac.uk/pdbsum/6gow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gow ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A162QQD4_BACIU A0A162QQD4_BACIU]] 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 == | |||
Flagellin is amongst the most abundant proteins in flagellated bacterial species and constitutes the major building block of the flagellar filament. The proteins FliW and FliS serve in the post-transcriptional control of flagellin and guide the protein to the flagellar type III secretion system (fT3SS), respectively. Here, we present the high-resolution structure of FliS/flagellin heterodimer and show that FliS and FliW bind to opposing interfaces located at the N- and C-termini of flagellin. The FliS/flagellin/FliW heterotrimer is able to interact with FlhA-C suggesting that FliW and FliS are released during flagellin export. After release, FliW and FliS are recycled to execute a new round of post-transcriptional regulation and targeting. Taken together, our study provides a mechanism explaining how FliW and FliS synchronize the production of flagellin with the capacity of the fT3SS to secrete flagellin. | |||
FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis.,Altegoer F, Mukherjee S, Steinchen W, Bedrunka P, Linne U, Kearns DB, Bange G Sci Rep. 2018 Aug 1;8(1):11552. doi: 10.1038/s41598-018-29884-8. PMID:30068950<ref>PMID:30068950</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gow" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Altegoer, F]] | |||
[[Category: Bange, G]] | [[Category: Bange, G]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: Flagellum]] | |||
[[Category: Type-3-secretion]] | |||
Latest revision as of 10:34, 29 August 2018
Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121
Structural highlights
Function[A0A162QQD4_BACIU] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073] Publication Abstract from PubMedFlagellin is amongst the most abundant proteins in flagellated bacterial species and constitutes the major building block of the flagellar filament. The proteins FliW and FliS serve in the post-transcriptional control of flagellin and guide the protein to the flagellar type III secretion system (fT3SS), respectively. Here, we present the high-resolution structure of FliS/flagellin heterodimer and show that FliS and FliW bind to opposing interfaces located at the N- and C-termini of flagellin. The FliS/flagellin/FliW heterotrimer is able to interact with FlhA-C suggesting that FliW and FliS are released during flagellin export. After release, FliW and FliS are recycled to execute a new round of post-transcriptional regulation and targeting. Taken together, our study provides a mechanism explaining how FliW and FliS synchronize the production of flagellin with the capacity of the fT3SS to secrete flagellin. FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis.,Altegoer F, Mukherjee S, Steinchen W, Bedrunka P, Linne U, Kearns DB, Bange G Sci Rep. 2018 Aug 1;8(1):11552. doi: 10.1038/s41598-018-29884-8. PMID:30068950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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