Part:BBa_K2710000
His-Alpha Prefoldin
alpha-Prefoldin with His-Tag
Usage and Biology
Prefoldin is a hetero-hexameric chaperone protein consisting of two α and four β subunits1, which was isolated from the thermophilic bacteria Methanobacterium thermoautotrophicum2. As a result, prefoldin is stable at high temperatures, with a Tm ≥ 70°C2. This 85kDa molecular chaperone protein is self-assembling, and consists of six α-helix coiled-coils (with each subunit as a coiled coil) protruding from a double β-barrel3. Each α subunit forms two β hairpins, and the four β hairpins from the two α subunits forms the two 8-stranded up and down β barrels2. Additionally, each β subunit forms one β hairpin. The subunits are anchored to the barrel via their proximal ends, and are fully solvated2. The α subunits are 85 Angstrom in height, and the β subunits are 70 Angstrom in height, with an overall distance of 50 Angstrom across the double β-barrel2. Sigert’s research also suggests that the coiled coils are flexible, although the overall structure is highly conserved2. Prefoldin is a molecular chaperone which, in archaea, carries out ‘de novo protein folding’, and in eukaryotes assists in the biogenesis of cytoskeletal proteins, thanks to its coiled coil ‘tentacles’1. We, however, are using it as the backbone to our modular, thermostable enzyme scaffold.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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