5iv7
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate== | |
+ | <SX load='5iv7' size='340' side='right' viewer='molstar' caption='[[5iv7]], [[Resolution|resolution]] 6.77Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5iv7]] is a 96 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=5IV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IV7 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]] 6.77Å</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=5iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iv7 OCA], [https://pdbe.org/5iv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iv7 RCSB], [https://www.ebi.ac.uk/pdbsum/5iv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iv7 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<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> |
+ | <div class="pdbe-citations 5iv7" 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 star-shaped, hubless post-attachment T4 baseplate
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