Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly.
The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol. TEM study suggested that this assembly is a regular dodecahedron, containing 12 Prx-2 decamers (Mr 2.62 MDa, external diameter approximately 20 nm). This interpretation has been supported by production of a approximately 1.6 nm 3D reconstruction from the negative stain TEM data, with automated docking of the available X-ray data of the Prx-2 decamer. Comparison with other known protein dodecahedral and viral icosahedral structures indicates that this arrangement of protein molecules is one of the fundamental macromolecular higher-order assemblies found in biology. Widespread biotechnological interest in macromolecular "cage" structures is relevant to the production of the Prx-2 dodecahedron.
Meissner
Ulrich
U
Institute of Zoology, University of Mainz, D-55099 Mainz, Germany.
Schröder
Ewald
E
Scheffler
Dirk
D
Martin
Andreas G
AG
Harris
J Robin
JR
D004912:Erythrocytes / Q000737:chemistry*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D046911:Macromolecular Substances; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D010544:Peroxidases / Q000737:chemistry*; D054464:Peroxiredoxins; D020836:Protein Structure, Quaternary
D046911:Macromolecular Substances; D010544:Peroxidases; D054464:Peroxiredoxins