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Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule

MarR family proteins regulate the transcription of multiple antibiotic-resistance genes and are widely found in bacteria and archaea. Recently, a new MarR family gene was identified by genome analysis of the psychrophilic bacterium Paenisporosarcina sp. TG-14, which was isolated from sediment-laden...

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Autores principales: Hwang, Jisub, Park, Sun-Ha, Lee, Chang Woo, Do, Hackwon, Shin, Seung Chul, Kim, Han-Woo, Lee, Sung Gu, Park, Hyun Ho, Kwon, Sunghark, Lee, Jun Hyuck
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/
https://www.ncbi.nlm.nih.gov/pubmed/34584745
http://dx.doi.org/10.1107/S2052252521005704
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author Hwang, Jisub
Park, Sun-Ha
Lee, Chang Woo
Do, Hackwon
Shin, Seung Chul
Kim, Han-Woo
Lee, Sung Gu
Park, Hyun Ho
Kwon, Sunghark
Lee, Jun Hyuck
author_facet Hwang, Jisub
Park, Sun-Ha
Lee, Chang Woo
Do, Hackwon
Shin, Seung Chul
Kim, Han-Woo
Lee, Sung Gu
Park, Hyun Ho
Kwon, Sunghark
Lee, Jun Hyuck
author_sort Hwang, Jisub
collection PubMed
description MarR family proteins regulate the transcription of multiple antibiotic-resistance genes and are widely found in bacteria and archaea. Recently, a new MarR family gene was identified by genome analysis of the psychrophilic bacterium Paenisporosarcina sp. TG-14, which was isolated from sediment-laden basal ice in Antarctica. In this study, the crystal structure of the MarR protein from Paenisporosarcina sp. TG-14 (PaMarR) was determined at 1.6 Å resolution. In the crystal structure, a novel lipid-type compound (palmitic acid) was found in a deep cavity, which was assumed to be an effector-binding site. Comparative structural analysis of homologous MarR family proteins from a mesophile and a hyperthermophile showed that the DNA-binding domain of PaMarR exhibited relatively high mobility, with a disordered region between the β1 and β2 strands. In addition, structural comparison with other homologous complex structures suggests that this structure constitutes a conformer transformed by palmitic acid. Biochemical analysis also demonstrated that PaMarR binds to cognate DNA, where PaMarR is known to recognize two putative binding sites depending on its molar concentration, indicating that PaMarR binds to its cognate DNA in a stoichiometric manner. The present study provides structural information on the cold-adaptive MarR protein with an aliphatic compound as its putative effector, extending the scope of MarR family protein research.
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spelling pubmed-84207662021-09-27 Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule Hwang, Jisub Park, Sun-Ha Lee, Chang Woo Do, Hackwon Shin, Seung Chul Kim, Han-Woo Lee, Sung Gu Park, Hyun Ho Kwon, Sunghark Lee, Jun Hyuck IUCrJ Research Papers MarR family proteins regulate the transcription of multiple antibiotic-resistance genes and are widely found in bacteria and archaea. Recently, a new MarR family gene was identified by genome analysis of the psychrophilic bacterium Paenisporosarcina sp. TG-14, which was isolated from sediment-laden basal ice in Antarctica. In this study, the crystal structure of the MarR protein from Paenisporosarcina sp. TG-14 (PaMarR) was determined at 1.6 Å resolution. In the crystal structure, a novel lipid-type compound (palmitic acid) was found in a deep cavity, which was assumed to be an effector-binding site. Comparative structural analysis of homologous MarR family proteins from a mesophile and a hyperthermophile showed that the DNA-binding domain of PaMarR exhibited relatively high mobility, with a disordered region between the β1 and β2 strands. In addition, structural comparison with other homologous complex structures suggests that this structure constitutes a conformer transformed by palmitic acid. Biochemical analysis also demonstrated that PaMarR binds to cognate DNA, where PaMarR is known to recognize two putative binding sites depending on its molar concentration, indicating that PaMarR binds to its cognate DNA in a stoichiometric manner. The present study provides structural information on the cold-adaptive MarR protein with an aliphatic compound as its putative effector, extending the scope of MarR family protein research. International Union of Crystallography 2021-09-01 /pmc/articles/PMC8420766/ /pubmed/34584745 http://dx.doi.org/10.1107/S2052252521005704 Text en © Jisub Hwang et al. 2021 https://creativecommons.org/licenses/by/4.0/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.
spellingShingle Research Papers
Hwang, Jisub
Park, Sun-Ha
Lee, Chang Woo
Do, Hackwon
Shin, Seung Chul
Kim, Han-Woo
Lee, Sung Gu
Park, Hyun Ho
Kwon, Sunghark
Lee, Jun Hyuck
Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title_full Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title_fullStr Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title_full_unstemmed Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title_short Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule
title_sort crystal structure of a marr family protein from the psychrophilic bacterium paenisporosarcina sp. tg-14 in complex with a lipid-like molecule
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/
https://www.ncbi.nlm.nih.gov/pubmed/34584745
http://dx.doi.org/10.1107/S2052252521005704
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