6Q12
Structure of pro-Esp mutant- S66V
Summary for 6Q12
| Entry DOI | 10.2210/pdb6q12/pdb |
| Related | 6PYM |
| Descriptor | Glutamyl endopeptidase (2 entities in total) |
| Functional Keywords | serine protease, hydrolase, zymogen |
| Biological source | Staphylococcus epidermidis (strain ATCC 12228) |
| Total number of polymer chains | 2 |
| Total formula weight | 55297.02 |
| Authors | Manne, K.,Narayana, S.V.L. (deposition date: 2019-08-02, release date: 2019-08-14, Last modification date: 2023-10-11) |
| Primary citation | Manne, K.,Narayana, S.V.L. Structural insights into the role of the N-terminus in the activation and function of extracellular serine protease from Staphylococcus epidermidis. Acta Crystallogr D Struct Biol, 76:28-40, 2020 Cited by PubMed Abstract: Extracellular serine protease (Esp) from Staphylococcus epidermidis is a glutamyl endopeptidase that inhibits the growth and formation of S. aureus biofilms. Previously, crystal structures of the matured and active Esp have been determined. Interestingly, many of the staphylococcal glutamyl endopeptidase zymogens, including V8 from Staphylococcus aureus and Esp from S. epidermidis, contain unusually long pro-peptide segments; however, their function is not known. With the aim of elucidating the function of these pro-peptide segments, crystal structures of the Esp zymogen (Pro-Esp) and its variants were determined. It was observed that the N-terminus of the Pro-Esp crystal structure is flexible and is not associated with the main body of the enzyme, unlike in the known active Esp structure. In addition, the loops that border the putative substrate-binding pocket of Pro-Esp are flexible and disordered; the structural components that are responsible for enzyme specificity and efficiency in serine proteases are disordered in Pro-Esp. However, the N-terminal locked Pro-Esp variants exhibit a rigid substrate-binding pocket similar to the active Esp structure and regain activity. These structural studies highlight the role of the N-terminus in stabilizing the structural components responsible for the activity and specificity of staphylococcal glutamyl endopeptidases. PubMed: 31909741DOI: 10.1107/S2059798319015055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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