Abstract
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 Ca2+, Mn2+, Fe2+/Fe3+, Co2+, Ni2+, Cu2+, Zn2+, and Cd2+, but not monovalent metal ions, Cr3+, Mg2+, Y3+, Sr2+ or Ba2+. 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.
Highlights
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
We present a crystallographic analysis of a recently discovered[8] tri-Asp metal-binding site on the three-fold symmetry axis of the hexameric LarE protein from Lactobacillus plantarum
An extensive database search for similar metal binding sites in other proteins resulted in only 13 hits and structural comparison among these sites revealed the uniqueness of the tri-Asp site in LarE
Summary
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. We present a crystallographic analysis of a recently discovered[8] tri-Asp metal-binding site on the three-fold symmetry axis of the hexameric LarE protein from Lactobacillus plantarum. An extensive database search for similar metal binding sites in other proteins resulted in only 13 hits and structural comparison among these sites revealed the uniqueness of the tri-Asp site in LarE.
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