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8gtb
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8gtb is ON HOLD Authors: Huang, Y., Sun, H., Wei, S., Zheng, Q., Li, S., Zhang, R., Xia, N. Description: Cryo-EM structure of the marine siphophage...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the marine siphophage vB_DshS-R4C tail tube protein== | |
| + | <StructureSection load='8gtb' size='340' side='right'caption='[[8gtb]], [[Resolution|resolution]] 3.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gtb]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Dinoroseobacter_phage_vB_DshS-R4C Dinoroseobacter phage vB_DshS-R4C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GTB 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]] 3.43Å</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=8gtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gtb OCA], [https://pdbe.org/8gtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gtb RCSB], [https://www.ebi.ac.uk/pdbsum/8gtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gtb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A4Y6EGR9_9CAUD A0A4Y6EGR9_9CAUD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tailed bacteriophages (order, Caudovirales) account for the majority of all phages. However, the long flexible tail of siphophages hinders comprehensive investigation of the mechanism of viral gene delivery. Here, we report the atomic capsid and in-situ structures of the tail machine of the marine siphophage, vB_DshS-R4C (R4C), which infects Roseobacter. The R4C virion, comprising 12 distinct structural protein components, has a unique five-fold vertex of the icosahedral capsid that allows genome delivery. The specific position and interaction pattern of the tail tube proteins determine the atypical long rigid tail of R4C, and further provide negative charge distribution within the tail tube. A ratchet mechanism assists in DNA transmission, which is initiated by an absorption device that structurally resembles the phage-like particle, RcGTA. Overall, these results provide in-depth knowledge into the intact structure and underlining DNA delivery mechanism for the ecologically important siphophages. | ||
| - | + | Structure and proposed DNA delivery mechanism of a marine roseophage.,Huang Y, Sun H, Wei S, Cai L, Liu L, Jiang Y, Xin J, Chen Z, Que Y, Kong Z, Li T, Yu H, Zhang J, Gu Y, Zheng Q, Li S, Zhang R, Xia N Nat Commun. 2023 Jun 17;14(1):3609. doi: 10.1038/s41467-023-39220-y. PMID:37330604<ref>PMID:37330604</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8gtb" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Dinoroseobacter phage vB_DshS-R4C]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Huang Y]] | ||
| + | [[Category: Li S]] | ||
| + | [[Category: Sun H]] | ||
| + | [[Category: Wei S]] | ||
| + | [[Category: Xia N]] | ||
| + | [[Category: Zhang R]] | ||
| + | [[Category: Zheng Q]] | ||
Current revision
Cryo-EM structure of the marine siphophage vB_DshS-R4C tail tube protein
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Categories: Dinoroseobacter phage vB DshS-R4C | Large Structures | Huang Y | Li S | Sun H | Wei S | Xia N | Zhang R | Zheng Q
