5a12

Crystal structure of Chlorite Dismutase from Magnetospirillum sp. in complex with azide

spinqualitylabelsall models 5a12, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a12 is a 5 chain structure with sequence from Magnetospirillum sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZI, GOL, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KL46_9PROT Publication Abstract from PubMed Chlorite dismutase (Cld) catalyzes the reduction of chlorite to chloride and dioxygen. Here, the ligand binding to Cld of Magnetospirillum sp. (MaCld) is investigated with X-ray crystallography and electron paramagnetic resonance (EPR). EPR reveals a large heterogeneity in the structure of wild-type MaCld, showing a variety of low- and high-spin ferric heme forms. Addition of an axial ligand, such as azide or imidazole, removes this heterogeneity almost entirely. This is in line with the two high resolution crystal structures of MaCld obtained in the presence of azide and thiocyanate that show the coordination of the ligands to the heme iron. The crystal structure of the MaCld-azide complex reveals a single well-defined orientation of the azide molecule in the heme pocket. EPR shows, however, a pH-dependent heme structure, probably due to acid-base transitions of the surrounding amino-acid residues stabilizing azide. For the azide and imidazole complex of MaCld, the hyperfine and nuclear quadrupole interactions with the close-by 14N and 1H nuclei are determined using pulsed EPR. These values are compared to the corresponding data for the low-spin forms observed in the ferric wild-type MaCld and to existing EPR data on azide and imidazole complexes of other heme proteins. Ligand Binding to Chlorite Dismutase from Magnetospirillum sp.,De Schutter A, Correia HD, Freire DM, Rivas MG, Rizzi A, Santos-Silva T, Gonzalez PJ, Van Doorslaer S J Phys Chem B. 2015 Aug 24. PMID:26287794 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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