5IV7
Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate
This is a non-PDB format compatible entry.
Summary for 5IV7
| Entry DOI | 10.2210/pdb5iv7/pdb |
| EMDB information | 3396 |
| Descriptor | Baseplate wedge protein gp6, Baseplate wedge protein gp7, Baseplate wedge protein gp8, ... (8 entities in total) |
| Functional Keywords | t4, baseplate, post-attachment, bacteriophage, bacterial virus, star-shaped, hubless, membrane-piercing, cell attachment, infection, viral protein |
| Biological source | Enterobacteria phage T4 More |
| Cellular location | Virion : P19060 P19061 P19062 P10927 P10928 P10929 P09425 P16011 |
| Total number of polymer chains | 96 |
| Total formula weight | 4473617.42 |
| 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: 2024-11-20) |
| 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 (6.77 Å) |
Structure validation
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