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

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 tha...

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Autores principales: Fellner, Matthias, Huizenga, Kamren G., Hausinger, Robert P., Hu, Jian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7118094/
https://www.ncbi.nlm.nih.gov/pubmed/32242052
http://dx.doi.org/10.1038/s41598-020-62847-6
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author Fellner, Matthias
Huizenga, Kamren G.
Hausinger, Robert P.
Hu, Jian
author_facet Fellner, Matthias
Huizenga, Kamren G.
Hausinger, Robert P.
Hu, Jian
author_sort Fellner, Matthias
collection PubMed
description 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.
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spelling pubmed-71180942020-04-06 Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE Fellner, Matthias Huizenga, Kamren G. Hausinger, Robert P. Hu, Jian Sci Rep Article 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. Nature Publishing Group UK 2020-04-02 /pmc/articles/PMC7118094/ /pubmed/32242052 http://dx.doi.org/10.1038/s41598-020-62847-6 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Fellner, Matthias
Huizenga, Kamren G.
Hausinger, Robert P.
Hu, Jian
Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title_full Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title_fullStr Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title_full_unstemmed Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title_short Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE
title_sort crystallographic characterization of a tri-asp metal-binding site at the three-fold symmetry axis of lare
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7118094/
https://www.ncbi.nlm.nih.gov/pubmed/32242052
http://dx.doi.org/10.1038/s41598-020-62847-6
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