Three-dimensional structure of a plant cardoon aspartic proteinase
نویسندگان
چکیده
منابع مشابه
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
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-te...
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Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The three-dimensional structure of two plant aspartic proteinases has been determined, sharing significant structural...
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The present article investigates the thermoelastic interaction in a three-dimensional homogeneous and isotropic sandwich structure using the dual-phase-lag (DPL) model of generalized thermoelasticity. The incorporated resulting non-dimensional coupled equations are applied to a specific problem in which a sandwich layer of unidentical homogeneous and isotropic substances is subjected to time-de...
متن کاملKNApSAcK-3D: a three-dimensional structure database of plant metabolites.
Studies on plant metabolites have attracted significant attention in recent years. Over the past 8 years, we have constructed a unique metabolite database, called KNApSAcK, that contains information on the relationships between metabolites and their expressing organism(s). In the present paper, we introduce KNApSAcK-3D, which contains the three-dimensional (3D) structures of all of the metaboli...
متن کاملCloning and characterization of cDNA encoding cardosin A, an RGD-containing plant aspartic proteinase.
Cardosin A is an abundant aspartic proteinase from pistils of Cynara cardunculus L. whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning and characterization of cardosin A cDNA. The deduced amino acid sequence contains the conserved features of plant aspartic proteinases, including the plant-specific insertion (PSI), and revealed the presence...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1996
ISSN: 0108-7673
DOI: 10.1107/s0108767396094974