1od5
From Proteopedia
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| , resolution 2.10Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF GLYCININ A3B4 SUBUNIT HOMOHEXAMER
Overview
Most plant seeds contain 11S globulins as major storage proteins for their nutrition. Soybean glycinin belongs to the 11S globulin family and consists of five kinds of subunits. We determined the crystal structure of a homohexamer of the glycinin A3B4 subunit at 2.1-A resolution. The crystal structure shows that the hexamer has 32-point group symmetry formed by face-to-face stacking of two trimers. The interface buries the highly conserved interchain disulfide. Based on the structure, we propose that an ingenious face-to-face mechanism controls the hexamer formation of the 11S globulin by movement of a mobile disordered region to the side of the trimer after posttranslational processing. Electrostatic analysis of the faces suggests that the interchain disulfide-containing face has high positive potential at acidic pH, which induces dissociation of the hexamer into trimers that may be susceptible to proteinases after seed imbibition. This dissociation might result in the degradation and mobilization of 11S globulins as storage proteins in embryos during germination and seedling growth.
About this Structure
1OD5 is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer., Adachi M, Kanamori J, Masuda T, Yagasaki K, Kitamura K, Mikami B, Utsumi S, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7395-400. Epub 2003 May 27. PMID:12771376
Page seeded by OCA on Sun Mar 30 22:43:29 2008
