1od5

From Proteopedia

Revision as of 11:31, 30 October 2007

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 ... [(full description)]

About this Structure

1OD5 is a [Single protein] structure of sequence from [Glycine max] with CO3 and MG as [ligands]. Structure known Active Site: AC1. 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

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