Tetrahedral aminopeptidase: a novel large protease complex from archaea.

@article{Franzetti2002TetrahedralAA,
  title={Tetrahedral aminopeptidase: a novel large protease complex from archaea.},
  author={Bruno Franzetti and Guy Schoehn and J Hern{\'a}ndez and Michel Jaquinod and Rob W. H. Ruigrok and Giuseppe Zaccai},
  journal={The EMBO journal},
  year={2002},
  volume={21 9},
  pages={2132-8}
}
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… CONTINUE READING

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