Structure of human uropepsin at 2.45 Å resolution

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 11; pp. 1560 - 1570
• Main Authors: Canduri, Fernanda, Teodoro, Lívia G. V. L., Fadel, Valmir, Lorenzi, Carla C. B., Hial, Valdemar, Gomes, Roseli A. S., Neto, João Ruggiero, De Azevedo Jr, Walter F.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-11-2001
• Subjects: Amino Acid Sequence; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Endopeptidases - chemistry; Humans; Models, Molecular; Molecular Sequence Data; Pepstatins - metabolism; Protein Conformation; Quality Control; Sequence Homology, Amino Acid; Substrate Specificity; uropepsin
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444901013865

The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P212121, with unit‐cell parameters a = 50.99, b = 75.56, c = 89.90 Å. Crystallographic refinement led to an R factor of 0.161 at 2.45 Å resolution. The positions of 2437 non‐H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly β‐sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo‐twofold axis. A model of the uropepsin–pepstatin complex has been constructed based on the high‐resolution crystal structure of pepsin complexed with pepstatin.