From Wikipedia, the free encyclopedia
A
trimer of the peridinin-chlorophyll-containing protein from the
dinoflagellate Amphidinium carterae illustrating the alpha solenoid fold. Bound
peridinin pigments are shown in pink and
chlorophyll in black.
An alpha solenoid is a protein fold found in the protein subunits of light-harvesting complexes, particularly in the peridinin chlorophyll proteins of dinoflagellates, and as domains of larger eukaryotic proteins that make up the nuclear pore complex. The fold consists of alpha helices arranged in a curved pattern that resembles a jelly roll fold. The extent of an alpha solenoid's curvature depends on the primary sequence; strongly curved solenoids have predictable sequence patterns and have led to the identification of probable solenoid-like components in the proteasome.
[edit] References
- Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K. (1996). Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae. Science 272(5269):1788-91.
- Devos D, Dokudovskaya S, Alber F, Williams R, Chait BT, Sali A, Rout MP. (2004). Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2(12):e380.
- Kajava AV. (2002). What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J Biol Chem 277(51):49791-8.
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