doi: 10.1006/jsbi.1999.4169.
Capsids of tricorn protease studied by electron cryomicroscopy
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- PMID: 10600560
- DOI: 10.1006/jsbi.1999.4169
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Capsids of tricorn protease studied by electron cryomicroscopy
J Struct Biol.
.
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.
Copyright 1999 Academic Press.
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