7ey8: Difference between revisions
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==portal== | ==portal== | ||
<StructureSection load='7ey8' size='340' side='right'caption='[[7ey8]]' scene=''> | <StructureSection load='7ey8' size='340' side='right'caption='[[7ey8]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EY8 FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EY8 FirstGlance]. <br> | ||
</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=7ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ey8 OCA], [https://pdbe.org/7ey8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ey8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ey8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ey8 ProSAT]</span></td></tr> | </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=7ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ey8 OCA], [https://pdbe.org/7ey8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ey8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ey8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ey8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many tailed bacteriophages assemble ejection proteins and a portal-tail complex at a unique vertex of the capsid. The ejection proteins form a transenvelope channel extending the portal-tail channel for the delivery of genomic DNA in cell infection. Here, we report the structure of the mature bacteriophage T7, including the ejection proteins, as well as the structures of the full and empty T7 particles in complex with their cell receptor lipopolysaccharide. Our near-atomic-resolution reconstruction shows that the ejection proteins in the mature T7 assemble into a core, which comprises a fourfold gene product 16 (gp16) ring, an eightfold gp15 ring, and a putative eightfold gp14 ring. The gp15 and gp16 are mainly composed of helix bundles, and gp16 harbors a lytic transglycosylase domain for degrading the bacterial peptidoglycan layer. When interacting with the lipopolysaccharide, the T7 tail nozzle opens. Six copies of gp14 anchor to the tail nozzle, extending the nozzle across the lipopolysaccharide lipid bilayer. The structures of gp15 and gp16 in the mature T7 suggest that they should undergo remarkable conformational changes to form the transenvelope channel. Hydrophobic alpha-helices were observed in gp16 but not in gp15, suggesting that gp15 forms the channel in the hydrophilic periplasm and gp16 forms the channel in the cytoplasmic membrane. | |||
Structural changes in bacteriophage T7 upon receptor-induced genome ejection.,Chen W, Xiao H, Wang L, Wang X, Tan Z, Han Z, Li X, Yang F, Liu Z, Song J, Liu H, Cheng L Proc Natl Acad Sci U S A. 2021 Sep 14;118(37). pii: 2102003118. doi:, 10.1073/pnas.2102003118. PMID:34504014<ref>PMID:34504014</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ey8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Portal protein 3D structures|Portal protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 08:09, 12 June 2024
portalportal
Structural highlights
Publication Abstract from PubMedMany tailed bacteriophages assemble ejection proteins and a portal-tail complex at a unique vertex of the capsid. The ejection proteins form a transenvelope channel extending the portal-tail channel for the delivery of genomic DNA in cell infection. Here, we report the structure of the mature bacteriophage T7, including the ejection proteins, as well as the structures of the full and empty T7 particles in complex with their cell receptor lipopolysaccharide. Our near-atomic-resolution reconstruction shows that the ejection proteins in the mature T7 assemble into a core, which comprises a fourfold gene product 16 (gp16) ring, an eightfold gp15 ring, and a putative eightfold gp14 ring. The gp15 and gp16 are mainly composed of helix bundles, and gp16 harbors a lytic transglycosylase domain for degrading the bacterial peptidoglycan layer. When interacting with the lipopolysaccharide, the T7 tail nozzle opens. Six copies of gp14 anchor to the tail nozzle, extending the nozzle across the lipopolysaccharide lipid bilayer. The structures of gp15 and gp16 in the mature T7 suggest that they should undergo remarkable conformational changes to form the transenvelope channel. Hydrophobic alpha-helices were observed in gp16 but not in gp15, suggesting that gp15 forms the channel in the hydrophilic periplasm and gp16 forms the channel in the cytoplasmic membrane. Structural changes in bacteriophage T7 upon receptor-induced genome ejection.,Chen W, Xiao H, Wang L, Wang X, Tan Z, Han Z, Li X, Yang F, Liu Z, Song J, Liu H, Cheng L Proc Natl Acad Sci U S A. 2021 Sep 14;118(37). pii: 2102003118. doi:, 10.1073/pnas.2102003118. PMID:34504014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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