2O8L
Structure of V8 protease from staphylococcus aureus
Summary for 2O8L
| Entry DOI | 10.2210/pdb2o8l/pdb |
| Related | 1QY6 |
| Descriptor | V8 protease, POTASSIUM ION (3 entities in total) |
| Functional Keywords | serine protease; enzyme, hydrolase |
| Biological source | Staphylococcus aureus |
| Cellular location | Secreted : Q99V45 |
| Total number of polymer chains | 1 |
| Total formula weight | 29714.79 |
| Authors | Delbaere, L.T.J.,Prasad, L.,Leduc, Y. (deposition date: 2006-12-12, release date: 2007-01-02, Last modification date: 2023-08-30) |
| Primary citation | Prasad, L.,Leduc, Y.,Hayakawa, K.,Delbaere, L.T.J. The Structure of a Universally Employed Enazyme: V8 Protease from Staphylococcus Aureus Acta Crystallogr.,Sect.D, 60:256-259, 2004 Cited by PubMed Abstract: 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. PubMed: 14747701DOI: 10.1107/S090744490302599X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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