2o8l
From Proteopedia
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Structure of V8 protease from staphylococcus aureus
Overview
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.
About this Structure
2O8L is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Active as Glutamyl endopeptidase, with EC number 3.4.21.19 Full crystallographic information is available from OCA.
Reference
The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus., Prasad L, Leduc Y, Hayakawa K, Delbaere LT, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):256-9. Epub 2004, Jan 23. PMID:14747701
Page seeded by OCA on Thu Feb 21 18:15:40 2008
