1PDP

Fitting of gp9 structure into the bacteriophage T4 baseplate cryoEM reconstruction

Summary for 1PDP

• Entry DOI: 10.2210/pdb1pdp/pdb
• Related: 1QEX
• EMDB information: 1048
• Descriptor: Baseplate structural protein Gp9 (1 entity in total)
• Functional Keywords: structural protein
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 18
• Total formula weight: 558445.05

Authors

Kostyuchenko, V.A.,Leiman, P.G.,Chipman, P.R.,Kanamaru, S.,van Raaij, M.J.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2003-05-19, release date: 2003-09-09, Last modification date: 2024-02-14)

Primary citation

Kostyuchenko, V.A.,Leiman, P.G.,Chipman, P.R.,Kanamaru, S.,van Raaij, M.J.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G.
Three-dimensional structure of the bacteriophage T4 baseplate
Nat.Struct.Biol., 10:688-693, 2003

PubMed 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.

PubMed: 12923574
DOI: 10.1038/nsb970

Experimental method

ELECTRON MICROSCOPY (12 Å)