Structural highlights
Function
PHSB_PHAVU Major seed storage protein.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.,Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM EMBO J. 1990 Jan;9(1):9-15. PMID:2295315[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM. The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution. EMBO J. 1990 Jan;9(1):9-15. PMID:2295315
