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| | ==Crystal Structure of flagellin assembly related protein== | | ==Crystal Structure of flagellin assembly related protein== |
| - | <StructureSection load='5gna' size='340' side='right' caption='[[5gna]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5gna' size='340' side='right'caption='[[5gna]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gna]] 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=5GNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GNA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gna]] is a 2 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GNA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliT, STM1962 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY]), fliD, flaV, flbC, STM1960 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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]] 2.3Å</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=5gna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gna OCA], [http://pdbe.org/5gna PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gna RCSB], [http://www.ebi.ac.uk/pdbsum/5gna PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gna 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=5gna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gna OCA], [https://pdbe.org/5gna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gna RCSB], [https://www.ebi.ac.uk/pdbsum/5gna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gna ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/FLID_SALTY FLID_SALTY]] Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | + | [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> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| | + | *[[Flagellar proteins|Flagellar proteins]] |
| | + | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Salty]] | + | [[Category: Large Structures]] |
| - | [[Category: Kim, H J]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Lee, H H]] | + | [[Category: Kim HJ]] |
| - | [[Category: Flagellin assembly related protein]] | + | [[Category: Lee HH]] |
| - | [[Category: Gene regulation]]
| + | |
| 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]
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
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