1PHS

THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION

Summary for 1PHS

• Entry DOI: 10.2210/pdb1phs/pdb
• Descriptor: PHASEOLIN, BETA-TYPE PRECURSOR (1 entity in total)
• Functional Keywords: plant seed storage protein (vicilin)
• Biological source: Phaseolus vulgaris
• Cellular location: Vacuole, aleurone grain: P02853
• Total number of polymer chains: 1
• Total formula weight: 45043.04

Authors

Lawrence, M.C.,Suzuki, E.,Varghese, J.N.,Davis, P.C.,Vandonkelaar, A.,Tulloch, P.A.,Colman, P.M. (deposition date: 1990-03-21, release date: 1990-10-15, Last modification date: 2023-09-27)

Primary citation

Lawrence, M.C.,Suzuki, E.,Varghese, J.N.,Davis, P.C.,Van Donkelaar, A.,Tulloch, P.A.,Colman, P.M.
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.
EMBO J., 9:9-15, 1990

PubMed 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.

PubMed: 2295315

Experimental method

X-RAY DIFFRACTION (3 Å)