title: Tetrahedral aminopeptidase: a novel large protease complex from archaea.
abstract: 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 all the proteolytic complexes described to date that are made up by rings or barrels with a single central channel and only two openings.
authors: Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France. franzetti@ibs.fr
authors: B
authors: B
authors: Franzetti
authors: G
authors: G
authors: Schoehn
authors: J-F
authors: JF
authors: Hernandez
authors: M
authors: M
authors: Jaquinod
authors: R W H
authors: RW
authors: Ruigrok
authors: G
authors: G
authors: Zaccai
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000502:physiology; D019843:Archaeal Proteins / Q000737:chemistry / Q000502:physiology; D019614:Haloarcula marismortui / Q000737:chemistry* / Q000502:physiology; D007473:Ion Channels / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D016415:Sequence Alignment; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D019843:Archaeal Proteins; D007473:Ion Channels; D046911:Macromolecular Substances; D021122:Protein Subunits; D000626:Aminopeptidases