8zvi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the bacteriophage T5 capsid== | |
| + | <StructureSection load='8zvi' size='340' side='right'caption='[[8zvi]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8zvi]] is a 14 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=8ZVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZVI 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]] 3.4Å</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=8zvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zvi OCA], [https://pdbe.org/8zvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zvi RCSB], [https://www.ebi.ac.uk/pdbsum/8zvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zvi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_BPT5 CAPSD_BPT5] Major capsid protein that self-associates to form 120 hexamers and 11 pentamers, building the T=13 icosahedral capsid which about 860 Angstroms in diameter. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function. The capsid gains its final stability through the reorganization of the subunits that takes place upon expansion. DNA encapsidation through the portal triggers capsid expansion and the binding of the decoration protein to the capsid exterior.<ref>PMID:20573812</ref> <ref>PMID:23500494</ref> <ref>PMID:26616586</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Liu | + | <div class="pdbe-citations 8zvi" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia phage T5]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu HR]] | ||
| + | [[Category: Peng Y]] | ||
Current revision
Structure of the bacteriophage T5 capsid
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