1QDM

CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.

1QDM の概要

• エントリーDOI: 10.2210/pdb1qdm/pdb
• 分子名称: PROPHYTEPSIN (1 entity in total)
• 機能のキーワード: aspartic proteinases, phytepsin, saposin-like domain, zymogen structure, hydrolase
• 由来する生物種: Hordeum vulgare
• 細胞内の位置: Vacuole: P42210
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 153985.21

構造登録者

Kervinen, J.,Tobin, G.J.,Costa, J.,Waugh, D.S.,Wlodawer, A.,Zdanov, A. (登録日: 1999-05-19, 公開日: 1999-07-16, 最終更新日: 2024-11-06)

主引用文献

Kervinen, J.,Tobin, G.J.,Costa, J.,Waugh, D.S.,Wlodawer, A.,Zdanov, A.
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
EMBO J., 18:3947-3955, 1999

PubMed Abstract: We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles.

PubMed: 10406799
DOI: 10.1093/emboj/18.14.3947

実験手法

X-RAY DIFFRACTION (2.3 Å)