5iv5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex== | |
| + | <SX load='5iv5' size='340' side='right' viewer='molstar' caption='[[5iv5]], [[Resolution|resolution]] 4.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5iv5]] is a 91 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IV5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.11Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5iv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iv5 OCA], [https://pdbe.org/5iv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iv5 RCSB], [https://www.ebi.ac.uk/pdbsum/5iv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iv5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BP07_BPT4 BP07_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:2254933</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> |
| + | <div class="pdbe-citations 5iv5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Goldie KN]] | ||
| + | [[Category: Guerrero-Ferreira RC]] | ||
| + | [[Category: Leiman PG]] | ||
| + | [[Category: Stahlberg H]] | ||
| + | [[Category: Taylor NMI]] | ||
Current revision
Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex
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