6ai2: Difference between revisions
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<StructureSection load='6ai2' size='340' side='right'caption='[[6ai2]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6ai2' size='340' side='right'caption='[[6ai2]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ai2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AI2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ai2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AI2 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a5i|3a5i]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a5i|3a5i]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flhA, STM1913 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=6ai2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ai2 OCA], [http://pdbe.org/6ai2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ai2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ai2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ai2 ProSAT]</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=6ai2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ai2 OCA], [http://pdbe.org/6ai2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ai2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ai2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ai2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FLHA_SALTY FLHA_SALTY]] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | [[http://www.uniprot.org/uniprot/FLHA_SALTY FLHA_SALTY]] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria use a type III protein export apparatus for construction of the flagellum, which consists of the basal body, the hook, and the filament. FlhA forms a homo-nonamer through its C-terminal cytoplasmic domains (FlhAC) and ensures the strict order of flagellar assembly. FlhAC goes through dynamic domain motions during protein export, but it remains unknown how it occurs. Here, we report that the FlhA(G368C) mutation biases FlhAC toward a closed form, thereby reducing the binding affinity of FlhAC for flagellar export chaperones in complex with their cognate filament-type substrates. The G368C mutations also restrict the conformational flexibility of a linker region of FlhA (FlhAL), suppressing FlhAC ring formation. We propose that interactions of FlhAL with its neighboring subunit converts FlhAC in the ring from a closed conformation to an open one, allowing the chaperon/substrate complexes to bind to the FlhAC ring to form the filament at the hook tip. | |||
Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus.,Inoue Y, Ogawa Y, Kinoshita M, Terahara N, Shimada M, Kodera N, Ando T, Namba K, Kitao A, Imada K, Minamino T Structure. 2019 Apr 16. pii: S0969-2126(19)30095-4. doi:, 10.1016/j.str.2019.03.017. PMID:31031200<ref>PMID:31031200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ai2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Salty]] | |||
[[Category: Imada, K]] | [[Category: Imada, K]] | ||
[[Category: Kinoshita, M]] | [[Category: Kinoshita, M]] | ||
Revision as of 11:08, 21 May 2019
Structure of the 328-692 fragment of FlhA (F459A)Structure of the 328-692 fragment of FlhA (F459A)
Structural highlights
Function[FLHA_SALTY] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. Publication Abstract from PubMedBacteria use a type III protein export apparatus for construction of the flagellum, which consists of the basal body, the hook, and the filament. FlhA forms a homo-nonamer through its C-terminal cytoplasmic domains (FlhAC) and ensures the strict order of flagellar assembly. FlhAC goes through dynamic domain motions during protein export, but it remains unknown how it occurs. Here, we report that the FlhA(G368C) mutation biases FlhAC toward a closed form, thereby reducing the binding affinity of FlhAC for flagellar export chaperones in complex with their cognate filament-type substrates. The G368C mutations also restrict the conformational flexibility of a linker region of FlhA (FlhAL), suppressing FlhAC ring formation. We propose that interactions of FlhAL with its neighboring subunit converts FlhAC in the ring from a closed conformation to an open one, allowing the chaperon/substrate complexes to bind to the FlhAC ring to form the filament at the hook tip. Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus.,Inoue Y, Ogawa Y, Kinoshita M, Terahara N, Shimada M, Kodera N, Ando T, Namba K, Kitao A, Imada K, Minamino T Structure. 2019 Apr 16. pii: S0969-2126(19)30095-4. doi:, 10.1016/j.str.2019.03.017. PMID:31031200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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