3tee: Difference between revisions

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==Crystal Structure of Salmonella FlgA in open form==

== Structural highlights ==

<table><tr><td colspan='2'>[[3tee]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar~~ typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEE FirstGlance]. <br>

<table><tr><td colspan='2'>[[3tee]] is a 1 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=3TEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEE FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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 ~~Salmonella enterica subsp. enterica serovar Typhimurium~~])</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='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=3tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tee RCSB], [http://www.ebi.ac.uk/pdbsum/3tee PDBsum]</span></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=3tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tee OCA], [http://pdbe.org/3tee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tee RCSB], [http://www.ebi.ac.uk/pdbsum/3tee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tee ProSAT]</span></td></tr>

</table>

== Function ==

[[http://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.

== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[User:Fadel A. Samatey/FlgA I|User:Fadel A. Samatey/FlgA I]]

== References ==

__TOC__

</StructureSection>

[[Category: ~~Salmonella enterica subsp. enterica serovar~~ typhimurium]]

[[Category: Bacillus typhimurium loeffler 1892]]

[[Category: Matsunami, H]]

[[Category: Namba, K]]

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@@ Line 1: / Line 1: @@
 ==Crystal Structure of Salmonella FlgA in open form==
 <StructureSection load='3tee' size='340' side='right' caption='[[3tee]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tee]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tee]] is a 1 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=3TEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEE FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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 Salmonella enterica subsp. enterica serovar Typhimurium])</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='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=3tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tee RCSB], [http://www.ebi.ac.uk/pdbsum/3tee PDBsum]</span></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=3tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tee OCA], [http://pdbe.org/3tee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tee RCSB], [http://www.ebi.ac.uk/pdbsum/3tee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tee ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://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 3tee" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[User:Fadel A. Samatey/FlgA I|User:Fadel A. Samatey/FlgA I]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
+[[Category: Bacillus typhimurium loeffler 1892]]
 [[Category: Matsunami, H]]
 [[Category: Namba, K]]