The three‐dimensional structure of the seed storage protein phaseolin at 3 A resolution

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...

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Bibliographic Details
Published in:The EMBO journal 1990-01, Vol.9 (1), p.9-15
Main Authors: Lawrence, M.C., Suzuki, E., Varghese, J.N., Davis, P.C., Van Donkelaar, A., Tulloch, P.A., Colman, P.M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Binding Sites
Biological and medical sciences
Crystallization
Fundamental and applied biological sciences. Psychology
Glycoproteins
Glycosylation
Macromolecular Substances
Molecular Sequence Data
Molecular Structure
Plant Proteins
Protein Conformation
Proteins
X-Ray Diffraction
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Summary: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.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1990.tb08074.x