View source for 6xgr


==YSD1 major tail protein==
<StructureSection load='6xgr' size='340' side='right'caption='[[6xgr]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xgr]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_sp. Bacteriophage sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XGR 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]] 3.5&#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=6xgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xgr OCA], [https://pdbe.org/6xgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xgr RCSB], [https://www.ebi.ac.uk/pdbsum/6xgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xgr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A498U5Z3_9CAUD A0A498U5Z3_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flagellotropic bacteriophages engage flagella to reach the bacterial surface as an effective means to increase the capture radius for predation. Structural details of these viruses are of great interest given the substantial drag forces and torques they face when moving down the spinning flagellum. We show that the main capsid and auxiliary proteins form two nested chainmails that ensure the integrity of the bacteriophage head. Core stabilising structures are conserved in herpesviruses suggesting their ancestral origin. The structure of the tail also reveals a robust yet pliable assembly. Hexameric rings of the tail-tube protein are braced by the N-terminus and a beta-hairpin loop, and interconnected along the tail by the splayed beta-hairpins. By contrast, we show that the beta-hairpin has an inhibitory role in the tail-tube precursor, preventing uncontrolled self-assembly. Dyads of acidic residues inside the tail-tube present regularly-spaced motifs well suited to DNA translocation into bacteria through the tail.

The architecture and stabilisation of flagellotropic tailed bacteriophages.,Hardy JM, Dunstan RA, Grinter R, Belousoff MJ, Wang J, Pickard D, Venugopal H, Dougan G, Lithgow T, Coulibaly F Nat Commun. 2020 Jul 27;11(1):3748. doi: 10.1038/s41467-020-17505-w. PMID:32719311<ref>PMID:32719311</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xgr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteriophage sp]]
[[Category: Large Structures]]
[[Category: Coulibaly FJ]]
[[Category: Dunstan R]]
[[Category: Hardy JM]]
[[Category: Lithgow TJ]]
[[Category: Venugopal H]]