Capsids of tricorn protease studied by electron cryomicroscopy |
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Authors: | Walz J Koster A J Tamura T Baumeister W |
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Institution: | Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Martinsried, 82152, Germany. |
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Abstract: | Tricorn protease from the archaeon Thermoplasma acidophilum acts "downstream" of the proteasome; in conjunction with its aminopeptidase cofactors it converts peptides generated by the proteasome into free amino acids. The basic functional unit of Tricorn is a homohexamer of the 121-kDa subunit, 20 of which can assemble further to form an icosahedral capsid with a molecular mass of 14.6 MDa. We have used electron cryomicroscopy to determine the structure of the Tricorn capsids to a resolution of 1.3 nm. |
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