5iw9: Difference between revisions
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New page: '''Unreleased structure''' The entry 5iw9 is ON HOLD Authors: Leiman, P.G., Browning, C., Shneider, M.M. Description: Structure of bacteriophage T4 gp25, sheath polymerization initiato... |
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==Structure of bacteriophage T4 gp25, sheath polymerization initiator== | |||
<StructureSection load='5iw9' size='340' side='right'caption='[[5iw9]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5iw9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hrz 4hrz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IW9 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]] 2.47Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5iw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iw9 OCA], [https://pdbe.org/5iw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iw9 RCSB], [https://www.ebi.ac.uk/pdbsum/5iw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iw9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BP25_BPT4 BP25_BPT4] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Browning | <div class="pdbe-citations 5iw9" style="background-color:#fffaf0;"></div> | ||
[[Category: Leiman | == References == | ||
[[Category: Shneider | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Browning C]] | |||
[[Category: Leiman PG]] | |||
[[Category: Shneider MM]] | |||
