7qyi
From Proteopedia
(Difference between revisions)
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<StructureSection load='7qyi' size='340' side='right'caption='[[7qyi]]' scene=''> | <StructureSection load='7qyi' size='340' side='right'caption='[[7qyi]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QYI FirstGlance]. <br> |
- | </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=7qyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qyi OCA], [https://pdbe.org/7qyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qyi RCSB], [https://www.ebi.ac.uk/pdbsum/7qyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qyi ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=7qyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qyi OCA], [https://pdbe.org/7qyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qyi RCSB], [https://www.ebi.ac.uk/pdbsum/7qyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qyi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [https://www.uniprot.org/uniprot/A0A2S6F8Q3_LEGPN A0A2S6F8Q3_LEGPN] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Naturally competent bacteria encode sophisticated protein machinery for the uptake and translocation of exogenous DNA into the cell. If this DNA is integrated into the bacterial genome, the bacterium is said to be naturally transformed. Most competent bacterial species utilise type IV pili for the initial DNA uptake step. These proteinaceous cell-surface structures are composed of thousands of pilus subunits (pilins), designated as major or minor according to their relative abundance in the pilus. Here, we show that the minor pilin FimT plays an important role in the natural transformation of Legionella pneumophila. We use NMR spectroscopy, in vitro DNA binding assays and in vivo transformation assays to understand the molecular basis of FimT's role in this process. FimT binds to DNA via an electropositive patch, rich in arginines, several of which are well-conserved and located in a conformationally flexible C-terminal tail. FimT orthologues from other Gammaproteobacteria share the ability to bind to DNA. Our results suggest that FimT plays an important role in DNA uptake in a wide range of competent species. | ||
- | + | ==See Also== | |
- | + | *[[Pilin 3D structures|Pilin 3D structures]] | |
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- | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Legionella pneumophila]] | ||
[[Category: Braus SAG]] | [[Category: Braus SAG]] | ||
[[Category: Gossert AD]] | [[Category: Gossert AD]] | ||
[[Category: Hospenthal MK]] | [[Category: Hospenthal MK]] |
Current revision
Solution structure of the DNA-binding minor pilin FimT from Legionella pneumophila
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