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| | <StructureSection load='5dmd' size='340' side='right'caption='[[5dmd]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='5dmd' size='340' side='right'caption='[[5dmd]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dmd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermodenitrificans"_klaushofer_and_hollaus_1970 "bacillus thermodenitrificans" klaushofer and hollaus 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DMD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DMD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dmd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DMD FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dmb|5dmb]]</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]] 1.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliW, GTNG_3059 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33940 "Bacillus thermodenitrificans" Klaushofer and Hollaus 1970])</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=5dmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dmd OCA], [https://pdbe.org/5dmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dmd RCSB], [https://www.ebi.ac.uk/pdbsum/5dmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dmd ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dmd OCA], [http://pdbe.org/5dmd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dmd RCSB], [http://www.ebi.ac.uk/pdbsum/5dmd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dmd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FLIW_GEOTN FLIW_GEOTN]] Binds to the C-terminal region of flagellin, which is implicated in polymerization, and participates in the assembly of the flagellum. | + | [https://www.uniprot.org/uniprot/FLIW_GEOTN FLIW_GEOTN] Binds to the C-terminal region of flagellin, which is implicated in polymerization, and participates in the assembly of the flagellum. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus thermodenitrificans klaushofer and hollaus 1970]] | + | [[Category: Geobacillus thermodenitrificans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altegoer, F]] | + | [[Category: Altegoer F]] |
| - | [[Category: Bange, G]] | + | [[Category: Bange G]] |
| - | [[Category: Assembly factor]]
| + | |
| - | [[Category: Flagellum]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
FLIW_GEOTN Binds to the C-terminal region of flagellin, which is implicated in polymerization, and participates in the assembly of the flagellum.
Publication Abstract from PubMed
Regulation of translation is critical for maintaining cellular protein levels, and thus protein homeostasis. The conserved RNA-binding protein CsrA (also called RsmA; for carbon storage regulator and regulator of secondary metabolism, respectively; hereafter called CsrA) represents a well-characterized example of regulation at the level of translation initiation in bacteria. Binding of a CsrA homodimer to the 5'UTR of an mRNA occludes the Shine-Dalgarno sequence, blocking ribosome access for translation. Small noncoding RNAs (sRNAs) can competitively antagonize CsrA activity by a well-understood mechanism. However, the regulation of CsrA by the protein FliW is just emerging. FliW antagonizes the CsrA-dependent repression of translation of the flagellar filament protein, flagellin. Crystal structures of the FliW monomer reveal a novel, minimal beta-barrel-like fold. Structural analysis of the CsrA/FliW heterotetramer shows that FliW interacts with a C-terminal extension of CsrA. In contrast to the competitive regulation of CsrA by sRNAs, FliW allosterically antagonizes CsrA in a noncompetitive manner by excluding the 5'UTR from the CsrA-RNA binding site. Our phylogenetic analysis shows that the FliW-mediated regulation of CsrA regulation is the ancestral state in flagellated bacteria. We thus demonstrate fundamental mechanistic differences in the regulation of CsrA by sRNA in comparison with an ancient regulatory protein.
Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein.,Altegoer F, Rensing SA, Bange G Proc Natl Acad Sci U S A. 2016 Sep 6;113(36):10168-73. doi:, 10.1073/pnas.1602425113. Epub 2016 Aug 22. PMID:27551070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Altegoer F, Rensing SA, Bange G. Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein. Proc Natl Acad Sci U S A. 2016 Sep 6;113(36):10168-73. doi:, 10.1073/pnas.1602425113. Epub 2016 Aug 22. PMID:27551070 doi:http://dx.doi.org/10.1073/pnas.1602425113
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