6533b825fe1ef96bd1282a0e

RESEARCH PRODUCT

Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly.

Ulrich MeissnerEwald SchröderAndreas G. MartinJ. Robin HarrisDirk Scheffler

subject

Models MolecularMaterials scienceErythrocytesIcosahedral symmetryMacromolecular SubstancesMacromolecular SubstancesGeneral Physics and AstronomyCell BiologyPeroxiredoxin 2Polyethylene glycolPeroxiredoxinsNegative stainDodecahedronCrystallographychemistry.chemical_compoundProtein structurechemistryMicroscopy Electron TransmissionPeroxidasesStructural BiologyImage Processing Computer-AssistedHumansGeneral Materials ScienceProtein Structure QuaternaryMacromolecule

description

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.

yearjournalcountryeditionlanguage
2004-03-14Micron (Oxford, England : 1993)
10.1016/j.micron.2006.04.010https://pubmed.ncbi.nlm.nih.gov/16839769