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Fitting of gp11 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 baseplate-tail tube complex
OverviewOverview
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.
About this StructureAbout this Structure
1PDF is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of bacteriophage T4 baseplate., Kostyuchenko VA, Leiman PG, Chipman PR, Kanamaru S, van Raaij MJ, Arisaka F, Mesyanzhinov VV, Rossmann MG, Nat Struct Biol. 2003 Sep;10(9):688-93. Epub 2003 Aug 17. PMID:12923574
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