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The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution
M C Lawrence1, E Suzuki, J N Varghese
1CSIRO Division of Biotechnology, Parkville, Victoria, Australia.
The EMBO Journal
|January 1, 1990
Abstract:
The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.