Tetrahedral aminopeptidase: a novel large protease complex from archaea.
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.
Franzetti
B
B
Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France. franzetti@ibs.fr
Schoehn
G
G
Hernandez
J-F
JF
Jaquinod
M
M
Ruigrok
R W H
RW
Zaccai
G
G
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
D019843:Archaeal Proteins; D007473:Ion Channels; D046911:Macromolecular Substances; D021122:Protein Subunits; D000626:Aminopeptidases