View source for 2rrl


==Solution structure of the C-terminal domain of the FliK==
<StructureSection load='2rrl' size='340' side='right'caption='[[2rrl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rrl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2rrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrl OCA], [https://pdbe.org/2rrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrl RCSB], [https://www.ebi.ac.uk/pdbsum/2rrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLIK_SALTY FLIK_SALTY] Controls the length of the flagellar hook.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The flagellar cytoplasmic protein FliK controls hook elongation by two successive events: by determining hook length and by stopping the supply of hook protein. These two distinct roles are assigned to different parts of FliK: the N-terminal half (FliK(N)) determines length and the C-terminal half (FliK(C)) switches secretion from the hook protein to the filament protein. The interaction of FliK(C) with FlhB, the switchable secretion gate, triggers the switch. By NMR spectroscopy, we demonstrated that FliK is largely unstructured and determined the structure of a compact domain in FliK(C). The compact domain, denoted the FliK(C) core domain, consists of two alpha-helices, a beta-sheet with two parallel and two antiparallel strands, and several exposed loops. Based on the functional data obtained by a series of deletion mutants of the FliK(C) core domain, we constructed a model of the complex between the FliK(C) core domain and FlhB(C). The model suggested that one of the FliK(C) loops has a high probability of interacting with the C-terminal domain of FlhB (FlhB(C)) as the FliK molecule enters the secretion gate. We suggest that the autocleaved NPTH sequence in FlhB contacts loop 2 of FliK(C) to trigger the switching event. This contact is sterically prevented when NPTH is not cleaved. Thus, the structure of FliK provides insight into the mechanism by which this bifunctional protein triggers a switch in the export of substrates.

The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.,Mizuno S, Amida H, Kobayashi N, Aizawa SI, Tate SI J Mol Biol. 2011 Apr 12. PMID:21510958<ref>PMID:21510958</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rrl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Amida H]]
[[Category: Kobayashi N]]
[[Category: Mizuno S]]
[[Category: Tate S]]