1IPJ

CRYSTAL STRUCTURES OF RECOMBINANT AND NATIVE SOYBEAN BETA-CONGLYCININ BETA HOMOTRIMERS COMPLEXES WITH N-ACETYL-D-GLUCOSAMINE

1IPJ の概要

• エントリーDOI: 10.2210/pdb1ipj/pdb
• 関連するPDBエントリー: 1IPK
• 分子名称: BETA-CONGLYCININ, BETA CHAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: soybean, storage protein, vicilin, sugar binding protein
• 由来する生物種: Glycine max (soybean)
• 細胞内の位置: Vacuole, aleurone grain : P25974
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 144560.01

構造登録者

Maruyama, N.,Adachi, M.,Takahashi, K.,Yagasaki, K.,Kohno, M.,Takenaka, Y.,Okuda, E.,Nakagawa, S.,Mikami, B.,Utsumi, S. (登録日: 2001-05-16, 公開日: 2002-05-16, 最終更新日: 2024-10-09)

主引用文献

Maruyama, N.,Adachi, M.,Takahashi, K.,Yagasaki, K.,Kohno, M.,Takenaka, Y.,Okuda, E.,Nakagawa, S.,Mikami, B.,Utsumi, S.
Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers.
Eur.J.Biochem., 268:3595-3604, 2001

PubMed Abstract: The crystal structures of recombinant and native beta homotrimers of soybean beta-conglycinin were determined by X-ray crystallography at 2.7 and 2.8 A resolutions, respectively. The crystals of the recombinant and native beta homotrimers belong to space group P21 with cell parameters a = 80.51 A, b = 63.48 A, c = 131.43 A, and beta = 90.01 degrees and with cell parameters a = 82.78 A, b = 69.47 A, c = 125.33 A and beta = 97.22 degrees, respectively. The beta monomers consist of amino-terminal and carboxyl-terminal modules that are very similar to each other and are related by a pseudo-dyad axis. Each module of the beta monomer is subdivided into a core and a loop domain. These structural features of both beta homotrimers are consistent with those of canavalin and phaseolin, which are similar vicilin class proteins. The superposition of the models of the native and recombinant beta monomers shows a root mean square deviation of 0.43-0.51 A for 343 common Calpha atoms within 2.0 A. This result indicates that the N-linked glycans do not influence the final structure of the beta homotrimer. Comparison of the models of beta-conglycinin, phaseolin and canavalin indicates that beta-conglycinin resembles canavalin rather than phaseolin, and that canavalin and phaseolin differ the most among them. The evolutional relationships are discussed.

PubMed: 11422391
DOI: 10.1046/j.1432-1327.2001.02268.x

実験手法

X-RAY DIFFRACTION (2.7 Å)