Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
复制标题
DOI：
10.1093/emboj/18.14.3947
复制
发表时间：
1999-07-15
期刊：
影响因子：
11.4
通讯作者：
Zdanov, A
中科院分区：
文献类型：
--
作者：
Kervinen, J;Tobin, GJ;Zdanov, A
We determined at 2.3 Angstrom 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.
