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'''THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION''' | '''THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION''' | ||
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[[Category: Vandonkelaar, A.]] | [[Category: Vandonkelaar, A.]] | ||
[[Category: Varghese, J N.]] | [[Category: Varghese, J N.]] | ||
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Revision as of 02:05, 3 May 2008
THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1PHS is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 05:05:59 2008
