6xxe: Difference between revisions

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 </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=6xxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xxe OCA], [http://pdbe.org/6xxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xxe RCSB], [http://www.ebi.ac.uk/pdbsum/6xxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xxe ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.
+Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.,Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942<ref>PMID:32376942</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6xxe" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>