8vjh: Difference between revisions
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==Cryo-EM of tail-tip of bacteriophage Chi== | |||
<StructureSection load='8vjh' size='340' side='right'caption='[[8vjh]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8vjh]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Chivirus_chi Chivirus chi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VJH 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]] 4.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=8vjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vjh OCA], [https://pdbe.org/8vjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vjh RCSB], [https://www.ebi.ac.uk/pdbsum/8vjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vjh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M9NVD3_9CAUD M9NVD3_9CAUD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The flagellotropic bacteriophage chi (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil chi's nearly complete structure, encompassing capsid, neck, tail, and tail tip. While the capsid and tail resemble phage YSD1, the neck and tail tip reveal new proteins and their arrangement. The neck shows a unique conformation of the tail tube protein, forming a socket-like structure for attachment to the neck. The tail tip comprises four proteins, including distal tail protein (DTP), two baseplate hub proteins (BH1P and BH2P), and tail tip assembly protein (TAP) exhibiting minimal organization compared to other siphophages. Deviating from the consensus in other siphophages, DTP in chi forms a trimeric assembly, reducing tail symmetry from 6-fold to 3-fold at the tip. These findings illuminate the previously unexplored structural organization of chi's neck and tail tip. | |||
Cryo-EM structure of flagellotropic bacteriophage Chi.,Sonani RR, Esteves NC, Scharf BE, Egelman EH Structure. 2024 Jul 11;32(7):856-865.e3. doi: 10.1016/j.str.2024.03.011. Epub , 2024 Apr 12. PMID:38614087<ref>PMID:38614087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8vjh" style="background-color:#fffaf0;"></div> | ||
[[Category: Esteves | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Chivirus chi]] | |||
[[Category: Large Structures]] | |||
[[Category: Egelman EH]] | |||
[[Category: Esteves NC]] | |||
[[Category: Scharf BE]] | |||
[[Category: Sonani RR]] | |||
Latest revision as of 06:59, 5 October 2024
Cryo-EM of tail-tip of bacteriophage ChiCryo-EM of tail-tip of bacteriophage Chi
Structural highlights
FunctionPublication Abstract from PubMedThe flagellotropic bacteriophage chi (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil chi's nearly complete structure, encompassing capsid, neck, tail, and tail tip. While the capsid and tail resemble phage YSD1, the neck and tail tip reveal new proteins and their arrangement. The neck shows a unique conformation of the tail tube protein, forming a socket-like structure for attachment to the neck. The tail tip comprises four proteins, including distal tail protein (DTP), two baseplate hub proteins (BH1P and BH2P), and tail tip assembly protein (TAP) exhibiting minimal organization compared to other siphophages. Deviating from the consensus in other siphophages, DTP in chi forms a trimeric assembly, reducing tail symmetry from 6-fold to 3-fold at the tip. These findings illuminate the previously unexplored structural organization of chi's neck and tail tip. Cryo-EM structure of flagellotropic bacteriophage Chi.,Sonani RR, Esteves NC, Scharf BE, Egelman EH Structure. 2024 Jul 11;32(7):856-865.e3. doi: 10.1016/j.str.2024.03.011. Epub , 2024 Apr 12. PMID:38614087[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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