3WJM

Crystal structure of Bombyx mori Sp2/Sp3 heterohexamer

3WJM の概要

• エントリーDOI: 10.2210/pdb3wjm/pdb
• 分子名称: Arylphorin, Silkworm storage protein, alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: bombyx mori storage proteins, papain cleavage site, heterohexamer, oxygen transport
• 由来する生物種: Bombyx mori (silk moth, silkworm); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 505433.43

構造登録者

Yuan, Y.A.,Hou, Y. (登録日: 2013-10-11, 公開日: 2014-09-24, 最終更新日: 2024-10-30)

主引用文献

Hou, Y.,Li, J.,Li, Y.,Dong, Z.,Xia, Q.,Yuan, Y.A.
Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites
Protein Sci., 23:735-746, 2014

PubMed Abstract: In holometabolous insects, the accumulation and utilization of storage proteins (SPs), including arylphorins and methionine-rich proteins, are critical for the insect metamorphosis. SPs function as amino acids reserves, which are synthesized in fat body, secreted into the larval hemolymph and taken up by fat body shortly before pupation. However, the detailed molecular mechanisms of digestion and utilization of SPs during development are largely unknown. Here, we report the crystal structure of Bombyx mori arylphorins at 2.8 Å, which displays a heterohexameric structural arrangement formed by trimerization of dimers comprising two structural similar arylphorins. Our limited proteolysis assay and microarray data strongly suggest that papain-like proteases are the major players for B. mori arylphorins digestion in vitro and in vivo. Consistent with the biochemical data, dozens of papain cleavage sites are mapped on the surface of the heterohexameric structure of B. mori arylphorins. Hence, our results provide the insightful information to understand the metamorphosis of holometabolous insects at molecular level.

PubMed: 24639361
DOI: 10.1002/pro.2457

実験手法

X-RAY DIFFRACTION (2.8 Å)