5IV5
Cryo-electron microscopy structure of the hexagonal pre-attachment T4 baseplate-tail tube complex
This is a non-PDB format compatible entry.
Summary for 5IV5
| Entry DOI | 10.2210/pdb5iv5/pdb |
| EMDB information | 3374 |
| Descriptor | Baseplate wedge protein gp6, Baseplate tail-tube protein gp48, Baseplate wedge protein gp53, ... (17 entities in total) |
| Functional Keywords | t4, baseplate-tail tube complex, pre-attachment, bacteriophage, bacterial virus, hexagonal, membrane-piercing, cell attachment, infection, viral protein |
| Biological source | Enterobacteria phage T4 More |
| Cellular location | Virion : P19060 P13339 P16011 P13341 P16009 P17172 P39234 P19061 P19062 P10927 P10928 P10929 P10930 P13333 P09425 |
| Total number of polymer chains | 145 |
| Total formula weight | 6490098.88 |
| Authors | Taylor, N.M.I.,Guerrero-Ferreira, R.C.,Goldie, K.N.,Stahlberg, H.,Leiman, P.G. (deposition date: 2016-03-19, release date: 2016-05-18, Last modification date: 2024-11-06) |
| Primary citation | Taylor, N.M.,Prokhorov, N.S.,Guerrero-Ferreira, R.C.,Shneider, M.M.,Browning, C.,Goldie, K.N.,Stahlberg, H.,Leiman, P.G. Structure of the T4 baseplate and its function in triggering sheath contraction. Nature, 533:346-352, 2016 Cited by PubMed Abstract: 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. PubMed: 27193680DOI: 10.1038/nature17971 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.11 Å) |
Structure validation
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