2phl
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THE STRUCTURE OF PHASEOLIN AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR A COMMON VICILIN(SLASH)LEGUMIN STRUCTURE AND THE GENETIC ENGINEERING OF SEED STORAGE PROTEINS
OverviewOverview
The refinement to 2.2 A resolution of the three-dimensional structure of, the seed storage protein phaseolin from the French bean (Phaseolus, vulgaris) via an alternative crystal form is described. The refined, structure reveals details of the molecule hitherto unobserved and in, particular we identify the structural role of conserved residues within, the broader 7 S (vicilin) family of seed storage proteins. On this basis, we are able to postulate a canonical model for the structure of the 7 S, proteins. This model in turn provides a means for interpreting the, structure of the 11 S (legumin) family of seed storage proteins, for which, no X-ray diffraction data are available. The 11 S proteins are shown to, bear a much closer relationship to the 7 S proteins than was previously, recognized. The canonical model of the 7 S protein structure also provides, a basis for proposing engineered mutations of these proteins with the goal, of enhancing nutritional and functional properties.
About this StructureAbout this Structure
2PHL is a Single protein structure of sequence from Phaseolus vulgaris with NAG and PO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins., Lawrence MC, Izard T, Beuchat M, Blagrove RJ, Colman PM, J Mol Biol. 1994 May 20;238(5):748-76. PMID:8182747
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