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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International Union of Crystallography
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ftpubmed:oai:pubmedcentral.nih.gov:8420766 2023-05-15T13:39:34+02:00 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 2021-09-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/ http://www.ncbi.nlm.nih.gov/pubmed/34584745 https://doi.org/10.1107/S2052252521005704 en eng International Union of Crystallography http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/ http://www.ncbi.nlm.nih.gov/pubmed/34584745 http://dx.doi.org/10.1107/S2052252521005704 © 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. CC-BY IUCrJ Research Papers Text 2021 ftpubmed https://doi.org/10.1107/S2052252521005704 2021-10-03T00:35:53Z 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. Text Antarc* Antarctica PubMed Central (PMC) Marr ENVELOPE(52.117,52.117,-66.400,-66.400) IUCrJ 8 5 842 852 |
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Research Papers |
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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 |
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Research Papers |
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. |
format |
Text |
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 |
title |
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_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_sort |
crystal structure of a marr family protein from the psychrophilic bacterium paenisporosarcina sp. tg-14 in complex with a lipid-like molecule |
publisher |
International Union of Crystallography |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/ http://www.ncbi.nlm.nih.gov/pubmed/34584745 https://doi.org/10.1107/S2052252521005704 |
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ENVELOPE(52.117,52.117,-66.400,-66.400) |
geographic |
Marr |
geographic_facet |
Marr |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
IUCrJ |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8420766/ http://www.ncbi.nlm.nih.gov/pubmed/34584745 http://dx.doi.org/10.1107/S2052252521005704 |
op_rights |
© 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. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1107/S2052252521005704 |
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8 |
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5 |
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