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The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data
In Mycobacterium tuberculosis, the proX gene encodes a putative compatible solute-binding protein (MtProX). However, it was found through sequence alignment that the MtProX protein has very different ligand-binding residues compared with other compatible solute-binding proteins, implying that MtProX...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5894108/ https://www.ncbi.nlm.nih.gov/pubmed/29633971 http://dx.doi.org/10.1107/S2053230X18003771 |
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author | Zhao, Jian-Hong Chen, Jiang-Huai Wang, Yong Wang, Zhi-Ping He, Yong-Xing |
author_facet | Zhao, Jian-Hong Chen, Jiang-Huai Wang, Yong Wang, Zhi-Ping He, Yong-Xing |
author_sort | Zhao, Jian-Hong |
collection | PubMed |
description | In Mycobacterium tuberculosis, the proX gene encodes a putative compatible solute-binding protein (MtProX). However, it was found through sequence alignment that the MtProX protein has very different ligand-binding residues compared with other compatible solute-binding proteins, implying that MtProX may bind to ligands that are as yet uncharacterized. In this work, it was demonstrated that MtProX binds to polyphenols such as phloretin, monoacetylphloroglucinol and 2,4-dihydroxyacetophloroglucinol with dissociation constants between 20 and 70 µM. Crystals of MtProX were obtained using a precipitant consisting of 0.2 M NaCl, 0.1 M Tris pH 8.5, 25%(w/v) polyethylene glycol 3350. The crystals diffracted to 2.10 Å resolution and belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 90.17, c = 161.92 Å, α = β = γ = 90.0°. Assuming the presence of two MtProX molecules in the asymmetric unit, the Matthews coefficient was calculated to be 2.74 Å(3) Da(−1), which corresponds to a solvent content of 55%. |
format | Online Article Text |
id | pubmed-5894108 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-58941082018-04-13 The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data Zhao, Jian-Hong Chen, Jiang-Huai Wang, Yong Wang, Zhi-Ping He, Yong-Xing Acta Crystallogr F Struct Biol Commun Research Communications In Mycobacterium tuberculosis, the proX gene encodes a putative compatible solute-binding protein (MtProX). However, it was found through sequence alignment that the MtProX protein has very different ligand-binding residues compared with other compatible solute-binding proteins, implying that MtProX may bind to ligands that are as yet uncharacterized. In this work, it was demonstrated that MtProX binds to polyphenols such as phloretin, monoacetylphloroglucinol and 2,4-dihydroxyacetophloroglucinol with dissociation constants between 20 and 70 µM. Crystals of MtProX were obtained using a precipitant consisting of 0.2 M NaCl, 0.1 M Tris pH 8.5, 25%(w/v) polyethylene glycol 3350. The crystals diffracted to 2.10 Å resolution and belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 90.17, c = 161.92 Å, α = β = γ = 90.0°. Assuming the presence of two MtProX molecules in the asymmetric unit, the Matthews coefficient was calculated to be 2.74 Å(3) Da(−1), which corresponds to a solvent content of 55%. International Union of Crystallography 2018-03-23 /pmc/articles/PMC5894108/ /pubmed/29633971 http://dx.doi.org/10.1107/S2053230X18003771 Text en © Zhao et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Communications Zhao, Jian-Hong Chen, Jiang-Huai Wang, Yong Wang, Zhi-Ping He, Yong-Xing The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title | The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title_full | The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title_fullStr | The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title_full_unstemmed | The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title_short | The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data |
title_sort | putative compatible solute-binding protein prox from mycobacterium tuberculosis h37rv: biochemical characterization and crystallographic data |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5894108/ https://www.ncbi.nlm.nih.gov/pubmed/29633971 http://dx.doi.org/10.1107/S2053230X18003771 |
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