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5m9f

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==Structure of the two C-terminal domains of bacteriophage K gp144==
==Structure of the two C-terminal domains of bacteriophage K gp144==
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<StructureSection load='5m9f' size='340' side='right' caption='[[5m9f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5m9f' size='340' side='right'caption='[[5m9f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5m9f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M9F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5m9f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_virus_K Staphylococcus virus K]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M9F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9f OCA], [http://pdbe.org/5m9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m9f RCSB], [http://www.ebi.ac.uk/pdbsum/5m9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9f ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m9f OCA], [https://pdbe.org/5m9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m9f RCSB], [https://www.ebi.ac.uk/pdbsum/5m9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m9f ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q6Y7P9_BPPGK Q6Y7P9_BPPGK]
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Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with "double-layered" baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210 degrees rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome's release.
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Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate.,Novacek J, Siborova M, Benesik M, Pantucek R, Doskar J, Plevka P Proc Natl Acad Sci U S A. 2016 Aug 16;113(33):9351-6. doi:, 10.1073/pnas.1605883113. Epub 2016 Jul 28. PMID:27469164<ref>PMID:27469164</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5m9f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Liu, A]]
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[[Category: Large Structures]]
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[[Category: Nguyen, T H]]
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[[Category: Staphylococcus virus K]]
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[[Category: Raaij, M J.van]]
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[[Category: Liu A]]
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[[Category: Baseplate protein]]
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[[Category: Nguyen TH]]
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[[Category: Putative receptor-binding protein]]
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[[Category: Van Raaij MJ]]
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[[Category: Tip domain]]
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[[Category: Tower domain]]
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[[Category: Viral protein]]
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Current revision

Structure of the two C-terminal domains of bacteriophage K gp144

PDB ID 5m9f

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