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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