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Orcid Publication

Detalle de: Three-dimensional structure of bacteriophage T4 baseplate.

Title Three-dimensional structure of bacteriophage T4 baseplate.
Abstract

The baseplate of bacteriophage T4 is a multiprotein molecular machine that controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. We report here the three-dimensional structure of the baseplate-tail tube complex determined to a resolution of 12 A by cryoelectron microscopy. The baseplate has a six-fold symmetric, dome-like structure approximately 520 A in diameter and approximately 270 A long, assembled around a central hub. A 940 A-long and 96 A-diameter tail tube, coaxial with the hub, is connected to the top of the baseplate. At the center of the dome is a needle-like structure that was previously identified as a cell puncturing device. We have identified the locations of six proteins with known atomic structures, and established the position and shape of several other baseplate proteins. The baseplate structure suggests a mechanism of baseplate triggering and structural transition during the initial stages of T4 infection.

Apa Reference Kostyuchenko, V. A., Leiman, P. G., Chipman, P. R., Kanamaru, S., van Raaij, M. J., Arisaka, F., Mesyanzhinov, V. V., & Rossmann, M. G. (2003). Three-dimensional structure of bacteriophage T4 baseplate. Nature Structural & Molecular Biology, 10(9), 688–693. 10.1038/nsb970
Doi 10.1038/nsb970
Publication Date 17 Aug 2003
Publication Type Article
Researcher Mark van Raaij
Ontology Viromics
Research Groups Structural Biology of Virus Proteins
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