7o89 | pdb_00007o89

sulerythrin without metals (apo-state)

spinqualitylabelsall models 7o89, resolution 1.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7o89 is a 1 chain structure with sequence from Sulfurisphaera tokodaii str. 7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.16Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F9VPE5_SULTO Publication Abstract from PubMed Bimetallic active sites in enzymes catalyze small-molecule conversions that are among the top 10 challenges in chemistry. As different metal cofactors are typically incorporated in varying protein scaffolds, it is demanding to disentangle the individual contributions of the metal and the protein matrix to the activity. Here, we compared the structure, properties, and hydrogen peroxide reactivity of four homobimetallic cofactors (Mn(II)2, Fe(II)2, Co(II)2, Ni(II)2) that were reconstituted into a four-helix bundle protein. Reconstituted proteins were studied in solution and in crystals. All metals bind with high affinity and yield similar cofactor structures. Cofactor variants react with H2O2 but differ in their turnover rates, accumulated oxidation states, and trapped peroxide-bound intermediates. Varying the metal composition thus creates opportunities to tune the reactivity of the bimetallic cofactor and to study and functionalize reactive species. Bimetallic Mn, Fe, Co, and Ni Sites in a Four-Helix Bundle Protein: Metal Binding, Structure, and Peroxide Activation.,Jeoung JH, Runger S, Haumann M, Neumann B, Klemke F, Davis V, Fischer A, Dau H, Wollenberger U, Dobbek H Inorg Chem. 2021 Nov 10. doi: 10.1021/acs.inorgchem.1c01919. PMID:34757735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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