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| | ==Recognition and targeting mechanisms by chaperones in flagella assembly and operation== | | ==Recognition and targeting mechanisms by chaperones in flagella assembly and operation== |
| - | <StructureSection load='5ks6' size='340' side='right'caption='[[5ks6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5ks6' size='340' side='right'caption='[[5ks6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ks6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salty Salty]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KS6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ks6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KS6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5kp0|5kp0]], [[5krw|5krw]]</div></td></tr> | + | </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=5ks6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ks6 OCA], [https://pdbe.org/5ks6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ks6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ks6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ks6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliT, STM1962 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ks6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ks6 OCA], [https://pdbe.org/5ks6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ks6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ks6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ks6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FLIT_SALTY FLIT_SALTY]] Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.<ref>PMID:10320579</ref> <ref>PMID:10791024</ref> <ref>PMID:11169117</ref> <ref>PMID:16952964</ref>
| + | [https://www.uniprot.org/uniprot/FLIT_SALTY FLIT_SALTY] Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.<ref>PMID:10320579</ref> <ref>PMID:10791024</ref> <ref>PMID:11169117</ref> <ref>PMID:16952964</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Economou, A]] | + | [[Category: Economou A]] |
| - | [[Category: Kalodimos, C G]] | + | [[Category: Kalodimos CG]] |
| - | [[Category: Khanra, N K]] | + | [[Category: Khanra NK]] |
| - | [[Category: Rossi, P]] | + | [[Category: Rossi P]] |
| - | [[Category: Assembly factor]]
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| - | [[Category: Chaperone]]
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| - | [[Category: Flagella]]
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| Structural highlights
Function
FLIT_SALTY Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.[1] [2] [3] [4]
Publication Abstract from PubMed
The flagellum is a complex bacterial nanomachine that requires the proper assembly of several different proteins for its function. Dedicated chaperones are central in preventing aggregation or undesired interactions of flagellar proteins, including their targeting to the export gate. FliT is a key flagellar chaperone that binds to several flagellar proteins in the cytoplasm, including its cognate filament-capping protein FliD. We have determined the solution structure of the FliT chaperone in the free state and in complex with FliD and the flagellar ATPase FliI. FliT adopts a four-helix bundle and uses a hydrophobic surface formed by the first three helices to recognize its substrate proteins. We show that the fourth helix constitutes the binding site for FlhA, a membrane protein at the export gate. In the absence of a substrate protein FliT adopts an autoinhibited structure wherein both the binding sites for substrates and FlhA are occluded. Substrate binding to FliT activates the complex for FlhA binding and thus targeting of the chaperone-substrate complex to the export gate. The activation and targeting mechanisms reported for FliT appear to be shared among the other flagellar chaperones.
Recognition and targeting mechanisms by chaperones in flagellum assembly and operation.,Khanra N, Rossi P, Economou A, Kalodimos CG Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):9798-803. doi:, 10.1073/pnas.1607845113. Epub 2016 Aug 15. PMID:27528687[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fraser GM, Bennett JC, Hughes C. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol Microbiol. 1999 May;32(3):569-80. PMID:10320579
- ↑ Kutsukake K, Ikebe T, Yamamoto S. Two novel regulatory genes, fliT and fliZ, in the flagellar regulon of Salmonella. Genes Genet Syst. 1999 Dec;74(6):287-92. PMID:10791024
- ↑ Bennett JC, Thomas J, Fraser GM, Hughes C. Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol Microbiol. 2001 Feb;39(3):781-91. PMID:11169117
- ↑ Yamamoto S, Kutsukake K. FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium. J Bacteriol. 2006 Sep;188(18):6703-8. PMID:16952964 doi:http://dx.doi.org/10.1128/JB.00799-06
- ↑ Khanra N, Rossi P, Economou A, Kalodimos CG. Recognition and targeting mechanisms by chaperones in flagellum assembly and operation. Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):9798-803. doi:, 10.1073/pnas.1607845113. Epub 2016 Aug 15. PMID:27528687 doi:http://dx.doi.org/10.1073/pnas.1607845113
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