Capsids of tricorn protease studied by electron cryomicroscopy.

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.

journal_name

J Struct Biol

authors

Walz J,Koster AJ,Tamura T,Baumeister W

doi

10.1006/jsbi.1999.4169

keywords:

subject

Has Abstract

pub_date

1999-12-01 00:00:00

pages

65-8

issue

1

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(99)94169-2

journal_volume

128

pub_type

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