The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus.
V8 protease, an extracellular protease of Staphylococcus aureus, is related to the pancreatic serine proteases. The enzyme cleaves peptide bonds exclusively on the carbonyl side of aspartate and glutamate residues. Unlike the pancreatic serine proteases, V8 protease possesses no disulfide bridges. This is a major evolutionary difference, as all pancreatic proteases have at least two disulfide bridges. The structure of V8 protease shows structural similarity with several other serine proteases, specifically the epidermolytic toxins A and B from S. aureus and trypsin, in which the conformation of the active site is almost identical. V8 protease is also unique in that the positively charged N-terminus is involved in determining the substrate-specificity of the enzyme.
Prasad
Lata
L
Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada.
Leduc
Yvonne
Y
Hayakawa
Koto
K
Delbaere
Louis T J
LT
D001224:Aspartic Acid / Q000737:chemistry; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004220:Disulfides; D018698:Glutamic Acid / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012694:Serine / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000201:enzymology*; D014357:Trypsin / Q000737:chemistry; D014961:X-Ray Diffraction
D004220:Disulfides; D010455:Peptides; D001224:Aspartic Acid; D018698:Glutamic Acid; D012694:Serine; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin