PubMed:10406799 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":97},"obj":"Sentence"},{"id":"T2","span":{"begin":98,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":427},"obj":"Sentence"},{"id":"T4","span":{"begin":428,"end":580},"obj":"Sentence"},{"id":"T5","span":{"begin":581,"end":783},"obj":"Sentence"},{"id":"T6","span":{"begin":784,"end":940},"obj":"Sentence"}],"text":"Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.\nWe 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."}