Three-dimensional structure of bacteriophage T4 baseplate

Victor A. Kostyuchenko, Petr G. Leiman, Paul R. Chipman, Shuji Kanamaru, Mark J. Van Raaij, Fumio Arisaka, Vadim V. Mesyanzhinov, Michael G. Rossmann

Research output: Contribution to journalArticle

143 Scopus citations

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 Å by cryoelectron microscopy. The baseplate has a six-fold symmetric, dome-like structure ∼520 Å in diameter and ∼270 Å long, assembled around a central hub. A 940 Å-long and 96 Å-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.

Original languageEnglish (US)
Pages (from-to)688-693
Number of pages6
JournalNature Structural Biology
Volume10
Issue number9
DOIs
StatePublished - Sep 1 2003
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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    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 Biology, 10(9), 688-693. https://doi.org/10.1038/nsb970