Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE

Matthias Fellner; Kamren G Huizenga; Robert P Hausinger; Jian Hu; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

doi:10.1038/s41598-020-62847-6

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Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE

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Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE

Matthias Fellner, Kamren G Huizenga, Robert P Hausinger, Jian Hu and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Scientific reports, Vol.10(1), pp.5830-5830

02/04/2020

DOI: https://doi.org/10.1038/s41598-020-62847-6

Handle:

https://hdl.handle.net/10523/26226

Abstract

Aspartic Acid - metabolism

Bacterial Proteins - metabolism

Binding Sites - physiology

Crystallography

Ions - metabolism

Lactobacillus plantarum - metabolism

Metals - metabolism

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 , Mn , Fe /Fe , Co , Ni , Cu , Zn , and Cd , but not monovalent metal ions, Cr , Mg , Y , Sr or Ba . 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.

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Record Identifier: 9926514982501891
Title: Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
Creators: Matthias Fellner
Kamren G Huizenga
Robert P Hausinger
Jian Hu
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Publication Details: Scientific reports, Vol.10(1), pp.5830-5830
Academic Unit: Biochemistry
Grant note: R01 GM128959 / NIGMS NIH HHS
Date published ; e-published: 02/04/2020
Language: English
Resource Type ; Subtype: Journal article