1QDM

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

Summary for 1QDM

• Entry DOI: 10.2210/pdb1qdm/pdb
• Descriptor: PROPHYTEPSIN (1 entity in total)
• Functional Keywords: aspartic proteinases, phytepsin, saposin-like domain, zymogen structure, hydrolase
• Biological source: Hordeum vulgare
• Cellular location: Vacuole: P42210
• Total number of polymer chains: 3
• Total formula weight: 153985.21

Authors

Kervinen, J.,Tobin, G.J.,Costa, J.,Waugh, D.S.,Wlodawer, A.,Zdanov, A. (deposition date: 1999-05-19, release date: 1999-07-16, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)