6t17: Difference between revisions

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-'''Unreleased structure'''
-The entry 6t17 is ON HOLD
+==Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia==
+<SX load='6t17' size='340' side='right' viewer='molstar' caption='[[6t17]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6t17]] is a 44 chain structure with sequence from [https://en.wikipedia.org/wiki/Kurthia_sp._11kri321 Kurthia sp. 11kri321]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T17 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</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=6t17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t17 OCA], [https://pdbe.org/6t17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t17 RCSB], [https://www.ebi.ac.uk/pdbsum/6t17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t17 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0X9VHV9_9BACL A0A0X9VHV9_9BACL] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament's supercoil. So far, all studied functional filaments are composed of a mixture of L- and R-state flagellin monomers. Here we show in a study of the wild type Firmicute Kurthia sp., that curved, functional filaments can adopt a conformation in vivo that is closely related to a uniform, all-L-state. This sheds additional light on transitions of the flagellar supercoil and uniquely reveals the atomic structure of a wild-type flagellar filament in vivo, including six residues showing clearly densities of O-linked glycosylation.
-Authors: Blum, T.B., Abrahams, J.P.
+The wild-type flagellar filament of the Firmicute Kurthia at 2.8 A resolution in vivo.,Blum TB, Filippidou S, Fatton M, Junier P, Abrahams JP Sci Rep. 2019 Oct 18;9(1):14948. doi: 10.1038/s41598-019-51440-1. PMID:31628388<ref>PMID:31628388</ref>
-Description: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Abrahams, J.P]]
+<div class="pdbe-citations 6t17" style="background-color:#fffaf0;"></div>
-[[Category: Blum, T.B]]
+==See Also==
+*[[Flagellin 3D structures|Flagellin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Kurthia sp. 11kri321]]
+[[Category: Large Structures]]
+[[Category: Abrahams JP]]
+[[Category: Blum TB]]