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-Structure paper
Title | Structure of the T4 baseplate and its function in triggering sheath contraction. |
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Journal, issue, pages | Nature, Vol. 533, Issue 7603, Page 346-352, Year 2016 |
Publish date | May 19, 2016 |
![]() | Nicholas M I Taylor / Nikolai S Prokhorov / Ricardo C Guerrero-Ferreira / Mikhail M Shneider / Christopher Browning / Kenneth N Goldie / Henning Stahlberg / Petr G Leiman / ![]() ![]() |
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 ...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. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.47 - 6.77 Å |
Structure data | EMDB-3374, PDB-5iv5: ![]() EMDB-3392: ![]() EMDB-3393: ![]() EMDB-3394: ![]() EMDB-3395: EMDB-3396, PDB-5iv7: ![]() EMDB-3397: ![]() PDB-5iw9: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-FE: ![]() ChemComp-HOH: |
Source |
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