3NJK
D116A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis, at pH5.5
Summary for 3NJK
| Entry DOI | 10.2210/pdb3njk/pdb |
| Related | 3N55 3NJF 3NJG 3NJH 3NJI 3NJJ 3NJL 3NJM 3NJN |
| Descriptor | Peptidase, GLYCEROL (3 entities in total) |
| Functional Keywords | structural genomics, aspartic peptidase, autocatalysis, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase |
| Biological source | Shewanella oneidensis |
| Total number of polymer chains | 1 |
| Total formula weight | 13774.63 |
| Authors | Osipiuk, J.,Mulligan, R.,Bargassa, M.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2010-06-17, release date: 2010-07-21, Last modification date: 2023-09-06) |
| Primary citation | Osipiuk, J.,Mulligan, R.,Bargassa, M.,Hamilton, J.E.,Cunningham, M.A.,Joachimiak, A. Characterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase. J.Biol.Chem., 287:19452-19461, 2012 Cited by PubMed Abstract: The crystal structure of SO1698 protein from Shewanella oneidensis was determined by a SAD method and refined to 1.57 Å. The structure is a β sandwich that unexpectedly consists of two polypeptides; the N-terminal fragment includes residues 1-116, and the C-terminal one includes residues 117-125. Electron density also displayed the Lys-98 side chain covalently linked to Asp-116. The putative active site residues involved in self-cleavage were identified; point mutants were produced and characterized structurally and in a biochemical assay. Numerical simulations utilizing molecular dynamics and hybrid quantum/classical calculations suggest a mechanism involving activation of a water molecule coordinated by a catalytic aspartic acid. PubMed: 22493430DOI: 10.1074/jbc.M112.358069 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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