Proteasome: from structure to function.
During the past two years, significant progress has been made in understanding the structure and function of the proteasome. Recent work has revealed the three-dimensional structure of the 700 kDa proteolytic complex at atomic resolution and elucidated its novel catalytic mechanism. Close relationships to a number of other amino-terminal hydrolases have emerged, making the proteasomal subunits the prototype of this newly discovered structural superfamily.
Stock
D
D
Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany. stock@biochem.mpg.de
Nederlof
P M
PM
Seemüller
E
E
Baumeister
W
W
Huber
R
R
Löwe
J
J
D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000276:immunology / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D018448:Models, Immunological; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000276:immunology / Q000502:physiology*; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D017510:Protein Folding
D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex