8ed0: Difference between revisions
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==Cryo-EM Structure of the P74-26 Tail Tube== | |||
<StructureSection load='8ed0' size='340' side='right'caption='[[8ed0]], [[Resolution|resolution]] 2.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ed0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P74-26 Thermus virus P74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ED0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ED0 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=8ed0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ed0 OCA], [https://pdbe.org/8ed0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ed0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ed0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ed0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A7XXS2_BP742 A7XXS2_BP742] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tail tube assembly is an essential step in the lifecycle of long-tailed bacteriophages. Limited structural and biophysical information has impeded an understanding of assembly and stability of their long, flexible tail tubes. The hyperthermophilic phage P74-26 is particularly intriguing as it has the longest tail of any known virus (nearly 1 mum) and is the most thermostable known phage. Here, we use structures of the P74-26 tail tube along with an in vitro system for studying tube assembly kinetics to propose the first molecular model for the tail tube assembly of long-tailed phages. Our high resolution cryo-EM structure provides insight into how the P74-26 phage assembles through flexible loops that fit into neighboring rings through tight "ball-and-socket"-like interactions. Guided by this structure, and in combination with mutational, light scattering, and molecular dynamics simulations data, we propose a model for the assembly of conserved tube-like structures across phage and other entities possessing Tail Tube-like proteins. We propose that formation of a full ring promotes the adoption of a tube elongation-competent conformation among the flexible loops and their corresponding sockets, which is further stabilized by an adjacent ring. Tail assembly is controlled by the cooperative interaction of dynamic intra- and inter-ring contacts. Given the structural conservation among tail tube proteins and tail-like structures, our model can explain the mechanism of high-fidelity assembly of long, stable tubes. | |||
Conformational dynamics control assembly of an extremely long bacteriophage tail tube.,Agnello E, Pajak J, Liu X, Kelch BA J Biol Chem. 2023 Feb 13:103021. doi: 10.1016/j.jbc.2023.103021. PMID:36791911<ref>PMID:36791911</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ed0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus virus P74-26]] | |||
[[Category: Agnello E]] | |||
[[Category: Kelch B]] | |||
[[Category: Liu X]] | |||
[[Category: Pajak J]] | |||
