5lye: Difference between revisions
m Protected "5lye" [edit=sysop:move=sysop] |
No edit summary |
||
(6 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Re-refined structure of the bacteriophage T4 short tail fibre PDB entry 1H6W containing 71 additionally identified residues== | |||
<StructureSection load='5lye' size='340' side='right'caption='[[5lye]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lye]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T2 Escherichia virus T2]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1h6w 1h6w]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LYE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5lye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lye OCA], [https://pdbe.org/5lye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lye RCSB], [https://www.ebi.ac.uk/pdbsum/5lye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lye ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q38160_BPT2 Q38160_BPT2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Contractile tail bacteriophages, or myobacteriophages, use a sophisticated biomolecular structure to inject their genome into the bacterial host cell. This structure consists of a contractile sheath enveloping a rigid tube that is sharpened by a spike-shaped protein complex at its tip. The spike complex forms the centerpiece of a baseplate complex that terminates the sheath and the tube. The baseplate anchors the tail to the target cell membrane with the help of fibrous proteins emanating from it and triggers contraction of the sheath. The contracting sheath drives the tube with its spiky tip through the target cell membrane. Subsequently, the bacteriophage genome is injected through the tube. The structural transformation of the bacteriophage T4 baseplate upon binding to the host cell has been recently described in near-atomic detail. In this review we discuss structural elements and features of this mechanism that are likely to be conserved in all contractile injection systems (systems evolutionary and structurally related to contractile bacteriophage tails). These include the type VI secretion system (T6SS), which is used by bacteria to transfer effectors into other bacteria and into eukaryotic cells, and tailocins, a large family of contractile bacteriophage tail-like compounds that includes the P. aeruginosa R-type pyocins. This article is protected by copyright. All rights reserved. | |||
Contractile injection systems of bacteriophages and related systems.,Taylor NMI, van Raaij MJ, Leiman PG Mol Microbiol. 2018 Feb 5. doi: 10.1111/mmi.13921. PMID:29405518<ref>PMID:29405518</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Leiman | <div class="pdbe-citations 5lye" style="background-color:#fffaf0;"></div> | ||
[[Category: Taylor | == References == | ||
[[Category: Van Raaij | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T2]] | |||
[[Category: Large Structures]] | |||
[[Category: Leiman PG]] | |||
[[Category: Taylor NMI]] | |||
[[Category: Van Raaij MJ]] |
Latest revision as of 15:04, 9 May 2024
Re-refined structure of the bacteriophage T4 short tail fibre PDB entry 1H6W containing 71 additionally identified residuesRe-refined structure of the bacteriophage T4 short tail fibre PDB entry 1H6W containing 71 additionally identified residues
Structural highlights
FunctionPublication Abstract from PubMedContractile tail bacteriophages, or myobacteriophages, use a sophisticated biomolecular structure to inject their genome into the bacterial host cell. This structure consists of a contractile sheath enveloping a rigid tube that is sharpened by a spike-shaped protein complex at its tip. The spike complex forms the centerpiece of a baseplate complex that terminates the sheath and the tube. The baseplate anchors the tail to the target cell membrane with the help of fibrous proteins emanating from it and triggers contraction of the sheath. The contracting sheath drives the tube with its spiky tip through the target cell membrane. Subsequently, the bacteriophage genome is injected through the tube. The structural transformation of the bacteriophage T4 baseplate upon binding to the host cell has been recently described in near-atomic detail. In this review we discuss structural elements and features of this mechanism that are likely to be conserved in all contractile injection systems (systems evolutionary and structurally related to contractile bacteriophage tails). These include the type VI secretion system (T6SS), which is used by bacteria to transfer effectors into other bacteria and into eukaryotic cells, and tailocins, a large family of contractile bacteriophage tail-like compounds that includes the P. aeruginosa R-type pyocins. This article is protected by copyright. All rights reserved. Contractile injection systems of bacteriophages and related systems.,Taylor NMI, van Raaij MJ, Leiman PG Mol Microbiol. 2018 Feb 5. doi: 10.1111/mmi.13921. PMID:29405518[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|