View source for 9ilp


==Structure of the bacteriophage T5 portal complex==
<StructureSection load='9ilp' size='340' side='right'caption='[[9ilp]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ilp]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T5 Escherichia phage T5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ILP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ILP 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]] 3.4&#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=9ilp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ilp OCA], [https://pdbe.org/9ilp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ilp RCSB], [https://www.ebi.ac.uk/pdbsum/9ilp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ilp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HCP_BPT5 HCP_BPT5] Head completion protein that closes the capsid once the viral DNA has been packaged. Probably part of the head-tail connector by binding to the portal protein and to the tail completion protein.<ref>PMID:24198424</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, we used cryo-electron microscopy (cryo-EM) to determine the structures of mature T5 (a laboratory-adapted, fiberless T5 mutant) and urea-treated empty T5 (lacking the tip complex) at near-atomic resolutions. Atomic models of the head, connector complex, tail tube, and tail tip were built for mature T5, and atomic models of the connector complex, comprising the portal protein pb7, adaptor protein p144, and tail terminator protein p142, were built for urea-treated empty T5. Our findings revealed that the aforementioned proteins did not undergo global conformational changes before and after DNA ejection, indicating that these structural features were conserved among most myophages and siphophages. The present study elucidates the underlying mechanisms of siphophage infection and DNA ejection.

Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection.,Peng Y, Tang H, Xiao H, Chen W, Song J, Zheng J, Liu H Int J Mol Sci. 2024 Aug 3;25(15):8479. doi: 10.3390/ijms25158479. PMID:39126049<ref>PMID:39126049</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ilp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia phage T5]]
[[Category: Large Structures]]
[[Category: Liu HR]]
[[Category: Peng YN]]