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...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2018-04, Vol.74 (4), p.231-235
Hauptverfasser: Zhao, Jian-Hong, Chen, Jiang-Huai, Wang, Yong, Wang, Zhi-Ping, He, Yong-Xing
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container_title Acta crystallographica. Section F, Structural biology communications
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creator Zhao, Jian-Hong
Chen, Jiang-Huai
Wang, Yong
Wang, Zhi-Ping
He, Yong-Xing
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 P43212, 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 Å3 Da−1, which corresponds to a solvent content of 55%. The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis was found to bind polyphenols instead of betaine, choline or carnitine. X‐ray diffraction data were collected to 2.10 Å resolution.
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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 P43212, 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 Å3 Da−1, which corresponds to a solvent content of 55%. The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis was found to bind polyphenols instead of betaine, choline or carnitine. 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Section F, Structural biology communications</title><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><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 P43212, 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 Å3 Da−1, which corresponds to a solvent content of 55%. The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis was found to bind polyphenols instead of betaine, choline or carnitine. 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Section F, Structural biology communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Jian-Hong</au><au>Chen, Jiang-Huai</au><au>Wang, Yong</au><au>Wang, Zhi-Ping</au><au>He, Yong-Xing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data</atitle><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><date>2018-04</date><risdate>2018</risdate><volume>74</volume><issue>4</issue><spage>231</spage><epage>235</epage><pages>231-235</pages><issn>2053-230X</issn><eissn>2053-230X</eissn><abstract>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 P43212, 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 Å3 Da−1, which corresponds to a solvent content of 55%. The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis was found to bind polyphenols instead of betaine, choline or carnitine. X‐ray diffraction data were collected to 2.10 Å resolution.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>29633971</pmid><doi>10.1107/S2053230X18003771</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
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subjects ABC transporter
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Betaine - chemistry
Betaine - metabolism
Carnitine - chemistry
Carnitine - metabolism
Catalytic Domain
Choline - chemistry
Choline - metabolism
Compatibility
Crystallization
Crystallography
Crystallography, X-Ray
Crystals
Ligands
Lymphocytes B
Mathematical analysis
Models, Molecular
Mycobacterium tuberculosis
Mycobacterium tuberculosis - metabolism
Nucleotide sequence
Polyethylene glycol
Polyphenols
Polyphenols - chemistry
Polyphenols - metabolism
Protein Conformation
Proteins
ProX
Research Communications
Sequence Homology
Sodium chloride
substrate‐binding protein
Tuberculosis
title The putative compatible solute‐binding protein ProX from Mycobacterium tuberculosis H37Rv: biochemical characterization and crystallographic data
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