2PHL

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

2PHL の概要

• エントリーDOI: 10.2210/pdb2phl/pdb
• 分子名称: PHASEOLIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: plant seed storage protein(vicilin)
• 由来する生物種: Phaseolus vulgaris
• 細胞内の位置: Vacuole, aleurone grain: P02853
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 136077.64

構造登録者

Lawrence, M.C.,Izard, T.,Beuchat, M.,Blagrove, R.J.,Colman, P.M. (登録日: 1994-07-07, 公開日: 1994-09-30, 最終更新日: 2024-10-30)

主引用文献

Lawrence, M.C.,Izard, T.,Beuchat, M.,Blagrove, R.J.,Colman, P.M.
Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins.
J.Mol.Biol., 238:748-776, 1994

PubMed Abstract: 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.

PubMed: 8182747
DOI: 10.1006/jmbi.1994.1333

実験手法

X-RAY DIFFRACTION (2.2 Å)