View source for 4hud


==Structure of the bacteriophage T4 tail terminator protein, gp15.==
<StructureSection load='4hud' size='340' side='right'caption='[[4hud]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hud]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HUD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7001&#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=4hud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hud OCA], [https://pdbe.org/4hud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hud RCSB], [https://www.ebi.ac.uk/pdbsum/4hud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hud ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COMPL_BPT4 COMPL_BPT4] Stabilizes the tail sheath structure and acts as a connector between the end of tail and the portal vertex of the capsid.<ref>PMID:23434847</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers.

The Molecular Architecture of the Bacteriophage T4 Neck.,Fokine A, Zhang Z, Kanamaru S, Bowman VD, Aksyuk AA, Arisaka F, Rao VB, Rossmann MG J Mol Biol. 2013 Feb 19. pii: S0022-2836(13)00098-3. doi:, 10.1016/j.jmb.2013.02.012. PMID:23434847<ref>PMID:23434847</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hud" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Aksyuk A]]
[[Category: Arisaka F]]
[[Category: Bowman VD]]
[[Category: Fokine A]]
[[Category: Kanamaru S]]
[[Category: Rao VB]]
[[Category: Rossmann MG]]
[[Category: Zhang Z]]