2HI8
human formylglycine generating enzyme, C336S mutant, bromide co-crystallization
Summary for 2HI8
| Entry DOI | 10.2210/pdb2hi8/pdb |
| Descriptor | Sulfatase-modifying factor 1, CTPSR, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | hydrolase activator, protein binding, formylglycin generation, post-translational modification, endoplasmic reticulum, sulfatase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Endoplasmic reticulum lumen: Q8NBK3 |
| Total number of polymer chains | 2 |
| Total formula weight | 34412.83 |
| Authors | Rudolph, M.G.,Roeser, D. (deposition date: 2006-06-29, release date: 2007-05-01, Last modification date: 2024-10-30) |
| Primary citation | Roeser, D.,Schmidt, B.,Preusser-Kunze, A.,Rudolph, M.G. Probing the oxygen-binding site of the human formylglycine-generating enzyme using halide ions. Acta Crystallogr.,Sect.D, 63:621-627, 2007 Cited by PubMed Abstract: The catalytic residue in sulfatases is a unique formylglycine that is post-translationally generated by oxidation of a cysteine or serine precursor. Molecular oxygen oxidizes the cysteine precursor in eukaryotic sulfatases, a reaction that is catalysed by the formylglycine-generating enzyme FGE. Previously, FGE was crystallized in complex with a chloride ion which, based on its similar polarizability and hydrophobicity, indicates the site of molecular oxygen binding. Here, two structures of FGE in complex with bromide and iodide were determined in order to further delineate the volume and stereochemical restraints of the oxygen-binding site for potential reaction intermediates. Anomalous difference density maps unambiguously assigned the nature of the halide ions. Unexpectedly, data collected at a wavelength of 1.54 A from the iodide-containing crystal and data collected at a wavelength of 0.8 A from a bromide-containing crystal were sufficient for SIRAS phasing. PubMed: 17452787DOI: 10.1107/S0907444907009961 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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