3mix: Difference between revisions

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 ==Crystal structure of the cytosolic domain of B. subtilis FlhA==
-<StructureSection load='3mix' size='340' side='right' caption='[[3mix]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3mix' size='340' side='right'caption='[[3mix]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mix]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mix]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU16390, flhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=3mix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mix OCA], [http://pdbe.org/3mix PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mix RCSB], [http://www.ebi.ac.uk/pdbsum/3mix PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mix ProSAT]</span></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=3mix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mix OCA], [https://pdbe.org/3mix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mix RCSB], [https://www.ebi.ac.uk/pdbsum/3mix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mix ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FLHA_BACSU FLHA_BACSU]] Involved in the export of flagellum proteins.
+[https://www.uniprot.org/uniprot/FLHA_BACSU FLHA_BACSU] Involved in the export of flagellum proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mix ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Flagella are the bacterial organelles of motility and can play important roles in pathogenesis. Flagella biosynthesis requires the coordinated export of huge protein amounts from the cytosol to the nascent flagellar structure at the cell surface and employs a type III secretion system (T3SS). Here we show that the integral membrane protein FlhA from the gram-positive bacterium Bacillus subtilis acts as an adaptor for late export substrates at the T3SS. The major filament protein (flagellin) and the filament-cap protein (FliD) bind to the FlhA cytoplasmic domain (FlhA-C) only in complex with their cognate chaperones (FliS and FliT). To understand the molecular details of these interactions we determined the FlhA-C crystal structure at 2.3 A resolution. FlhA-C consists of an N-terminal linker region, three subdomains with a novel fold, and a disordered region essential for the adaptor function. We show that the export protein FliJ associates with the linker region and modulates the binding properties of FlhA-C. While the interaction of FliD/FliT is enhanced, flagellin/FliS is not affected. FliJ also keeps FliT associated with FlhA-C and excess of FliT inhibits binding of FliD/FliT, suggesting that empty FliT chaperones stay associated with FliJ after export of FliD. Taken together, these results allow to propose a model that explains how the T3SS may switch from the stoichiometric export of FliD to the high-throughput secretion of flagellin.
-FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system.,Bange G, Kummerer N, Engel C, Bozkurt G, Wild K, Sinning I Proc Natl Acad Sci U S A. 2010 Jun 2. PMID:20534509<ref>PMID:20534509</ref>
+==See Also==
+*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3mix" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacsu]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Bange, G]]
+[[Category: Large Structures]]
-[[Category: Bozkurt, G]]
+[[Category: Bange G]]
-[[Category: Kuemmerer, N]]
+[[Category: Bozkurt G]]
-[[Category: Sinning, I]]
+[[Category: Kuemmerer N]]
-[[Category: Wild, K]]
+[[Category: Sinning I]]
-[[Category: Flagella biosynthesis]]
+[[Category: Wild K]]
-[[Category: Protein transport]]
-[[Category: Type iii secretion]]