9x3q: Difference between revisions
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==Phage T4 inner baseplate in post-tail-contraction state (genome-full particle)== | |||
<StructureSection load='9x3q' size='340' side='right'caption='[[9x3q]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9x3q]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T4 Escherichia phage T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9X3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9X3Q 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]] 3.7Å</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=9x3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9x3q OCA], [https://pdbe.org/9x3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9x3q RCSB], [https://www.ebi.ac.uk/pdbsum/9x3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9x3q ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Myophage is endowed with a sophisticated contractile tail and infection machinery. However, the mechanisms of host recognition, signal transduction, and genome delivery remain poorly understood. Here, we capture a pre-genome-release intermediate of myophage T4 and determine its structure by cryo-electron microscopy. Comparative analysis of this tail-contracted, pre-genome-release intermediate structure with the mature T4 virion and the tail-contracted, post-genome-release structure reveals structural transitions in the tail, tape-measure protein (TMP), baseplate, and long tail fibers that drive genome delivery. Our findings further suggest that tail sheath contraction is coupled to a coordinated repositioning of the viral DNA-TMP complex, potentially facilitating genome translocation via charge-mediated interactions. It appears that the expelled TMP may further reorganize into a putative transmembrane complex that supports genome delivery into the host cytosol. | |||
Cryo-EM Structures of Phage T4 Infection Intermediate.,Shao Q, Dong J, Wang A, Hu H, Yue J, Li H, Li Y, Zhang Q, Liu J, Sun L, Fokine A, Rao VB, Tao P, Fang Q J Mol Biol. 2026 Jul 4;438(19):169938. doi: 10.1016/j.jmb.2026.169938. PMID:42401366<ref>PMID:42401366</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9x3q" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia phage T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Dong J]] | |||
[[Category: Fang Q]] | |||
[[Category: Fokine A]] | |||
[[Category: Hu H]] | |||
[[Category: Li H]] | |||
[[Category: Li Y]] | |||
[[Category: Liu J]] | |||
[[Category: Rao VB]] | |||
[[Category: Shao Q]] | |||
[[Category: Sun L]] | |||
[[Category: Tao P]] | |||
[[Category: Wang A]] | |||
[[Category: Yue J]] | |||
[[Category: Zhang Q]] | |||
Latest revision as of 16:27, 22 July 2026
Phage T4 inner baseplate in post-tail-contraction state (genome-full particle)
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