3n55

SO1698 protein, an aspartic peptidase from Shewanella oneidensis.

spinqualitylabelsall models 3n55, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3n55 is a 2 chain structure with sequence from Shewanella oneidensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Ligands: ACT, BME, MSE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8EGA7_SHEON 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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