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Journal Article

Capsids of tricorn protease studied by electron cryomicroscopy

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Walz, J., Koster, A. J., Tamura, T., & Baumeister, W. (1999). Capsids of tricorn protease studied by electron cryomicroscopy. Journal of Structural Biology, 128(1), 65-68.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-71A9-8
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. (C) 1999 Academic Press. [References: 16]