6utt | pdb_00006utt

LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with calcium

spinqualitylabelsall models 6utt, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6utt is a 6 chain structure with sequence from "lactobacillus_arabinosus"_fred_et_al. "lactobacillus arabinosus" fred et al.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, PO4, SO4 Gene: larE, AVR82_02840, BIZ32_00440, CFM86_00460, CUR48_11145, E3O64_03880, IV39_GL000116, LPJSA22_00116, LpLQ80_00490, Nizo1839_0768, Nizo2891_3302 ("Lactobacillus arabinosus" Fred et al.) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Detailed crystallographic characterization of a tri-aspartate metal-binding site previously identified on the three-fold symmetry axis of a hexameric enzyme, LarE from Lactobacillus plantarum, was conducted. By screening an array of monovalent, divalent, and trivalent metal ions, we demonstrated that this metal binding site stoichiometrically binds Ca(2+), Mn(2+), Fe(2+)/Fe(3+), Co(2+), Ni(2+), Cu(2+), Zn(2+), and Cd(2+), but not monovalent metal ions, Cr(3+), Mg(2+), Y(3+), Sr(2+) or Ba(2+). Extensive database searches resulted in only 13 similar metal binding sites in other proteins, indicative of the rareness of tri-aspartate architectures, which allows for engineering such a selective multivalent metal ion binding site into target macromolecules for structural and biophysical characterization. Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.,Fellner M, Huizenga KG, Hausinger RP, Hu J Sci Rep. 2020 Apr 2;10(1):5830. doi: 10.1038/s41598-020-62847-6. PMID:32242052 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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