Tetrahedral aminopeptidase: a novel large protease complex from archaea.
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ABSTRACT:
SUBMITTER: Franzetti B
PROVIDER: S-EPMC125989 | biostudies-literature | 2002 May
REPOSITORIES: biostudies-literature
Publications
Tetrahedral aminopeptidase: a novel large protease complex from archaea.
Franzetti B B Schoehn G G Hernandez J-F JF Jaquinod M M Ruigrok R W H RW Zaccai G G
The EMBO journal 20020501 9
A dodecameric protease complex with a tetrahedral shape (TET) was isolated from Haloarcula marismortui, a salt-loving archaeon. The 42 kDa monomers in the complex are homologous to metal-binding, bacterial aminopeptidases. TET has a broad aminopeptidase activity and can process peptides of up to 30-35 amino acids in length. TET has a central cavity that is accessible through four narrow channels (<17 A wide) and through four wider channels (21 A wide). This architecture is different from that of ...[more]
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