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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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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. |
format | Online Article Text |
id | pubmed-7118094 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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