6gow: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6gow is ON HOLD  until Paper Publication
+==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]] 2.10&Aring;' 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.
-Authors: Altegoer, F., Bange, G.
+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>
-Description: Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6gow" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Altegoer, F]]
 [[Category: Bange, G]]
-[[Category: Altegoer, F]]
+[[Category: Chaperone]]
+[[Category: Flagellum]]
+[[Category: Type-3-secretion]]