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Kostyuchenko, VA, Leiman, PG, Chipman, PR, Kanamaru, S, van Raaij, MJ, Arisaka, F, Mesyanzhinov, VV and Rossmann, MG (2003) Three-dimensional structure of bacteriophage T4 baseplate. Nat. Struct. Biol. 10:688-93
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.
Bacteriophage T4/chemistry; Bacteriophage T4/ultrastructure; Cryoelectron Microscopy; Image Processing, Computer-Assisted; Microscopy, Electron; Models, Molecular; Protein Structure, Tertiary
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0004170: dUTP diphosphatase activity||
catalyses the hydrolysis of dUTP to dUMP and PPi and involved in the removal of dUTP from the dNTP pool, thus preventing this nucleotide from being available for DNA polymerase
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