5lye: Difference between revisions

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'''Unreleased structure'''


The entry 5lye is ON HOLD  until Paper Publication
==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]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lye]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LYE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h6w|1h6w]], [[5iv5|5iv5]]</td></tr>
<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=5lye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lye OCA], [http://pdbe.org/5lye PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lye RCSB], [http://www.ebi.ac.uk/pdbsum/5lye PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lye ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.


Authors: van Raaij, M.J., Taylor, N.M.I., Leiman, P.G.
Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680<ref>PMID:27193680</ref>


Description: Re-refined structure of the bacteriophage T4 short tail fibre PDB entry 1H6W containing 71 additionally identified residues
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Van Raaij, M.J]]
<div class="pdbe-citations 5lye" style="background-color:#fffaf0;"></div>
[[Category: Leiman, P.G]]
== References ==
[[Category: Taylor, N.M.I]]
<references/>
__TOC__
</StructureSection>
[[Category: Leiman, P G]]
[[Category: Raaij, M J.van]]
[[Category: Taylor, N M.I]]
[[Category: Adhesin]]
[[Category: Fibrous protein]]
[[Category: Gene product 12]]
[[Category: Structural protein]]
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