Structure of human uropepsin at 2.45 A resolution.
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 P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A 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 beta-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.
Canduri
F
F
Departamento de Física, IBILCE, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Teodoro
L G
LG
Fadel
V
V
Lorenzi
C C
CC
Hial
V
V
Gomes
R A
RA
Neto
J R
JR
de Azevedo
W F
WF
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010436:Pepstatins / Q000378:metabolism; D011487:Protein Conformation; D011786:Quality Control; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D010436:Pepstatins; D010450:Endopeptidases; C100308:uropepsin; C031375:pepstatin