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The three‐dimensional structure of the seed storage protein phaseolin at 3 A resolution.
Author(s) -
Lawrence M.C.,
Suzuki E.,
Varghese J.N.,
Davis P.C.,
Van Donkelaar A.,
Tulloch P.A.,
Colman P.M.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08074.x
Subject(s) - biology , storage protein , biochemistry , gene
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.