Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of SO1698 protein from Shewanella oneidensis was determined by a SAD method and refined to 1.57 A. The structure is a beta 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.
Characterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase.,Osipiuk J, Mulligan R, Bargassa M, Hamilton JE, Cunningham MA, Joachimiak A J Biol Chem. 2012 Jun 1;287(23):19452-61. Epub 2012 Apr 5. PMID:22493430[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Osipiuk J, Mulligan R, Bargassa M, Hamilton JE, Cunningham MA, Joachimiak A. Characterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase. J Biol Chem. 2012 Jun 1;287(23):19452-61. Epub 2012 Apr 5. PMID:22493430 doi:http://dx.doi.org/10.1074/jbc.M112.358069
