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==Orthorhombic Crystal Structure of Salmonella FlgA in closed form==
==Orthorhombic Crystal Structure of Salmonella FlgA in closed form==
<StructureSection load='3vjp' size='340' side='right' caption='[[3vjp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3vjp' size='340' side='right'caption='[[3vjp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vjp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VJP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3vjp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VJP FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tee|3tee]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tee|3tee]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flgA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=3vjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vjp RCSB], [http://www.ebi.ac.uk/pdbsum/3vjp PDBsum]</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=3vjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vjp OCA], [https://pdbe.org/3vjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vjp RCSB], [https://www.ebi.ac.uk/pdbsum/3vjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vjp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/FLGA_SALTY FLGA_SALTY]] Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain. Pull-down experiments support a specific protein-protein interaction between FlgI, the P-ring component protein, and the C-terminal domain of FlgA. Surface plasmon resonance and limited-proteolysis indicate that flexibility of the domain is reduced in the covalently closed form. These results show that the structural flexibility of the C-terminal domain of FlgA, which is related to the structural difference between the two crystal forms, is intrinsically associated with its molecular chaperone function in P-ring assembly.
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.,Matsunami H, Yoon YH, Meshcheryakov VA, Namba K, Samatey FA Sci Rep. 2016 Jun 7;6:27399. doi: 10.1038/srep27399. PMID:27273476<ref>PMID:27273476</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vjp" style="background-color:#fffaf0;"></div>
==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
*[[Flagellar proteins|Flagellar proteins]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Large Structures]]
[[Category: Matsunami, H]]
[[Category: Matsunami, H]]
[[Category: Namba, K]]
[[Category: Namba, K]]
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