The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism
Transcriptional regulator proteins are closely involved in essential survival strategies in bacteria. AcrR is a one‐component allosteric repressor of the genes associated with lipid transport and antibiotic resistance. When fatty acid ligands bind to the C‐terminal ligand‐binding cavity of AcrR, a c...
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| Format: | Article |
| Language: | English |
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Wiley
2019-10-01
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| Series: | FEBS Open Bio |
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| Online Access: | https://doi.org/10.1002/2211-5463.12710 |
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| author | Sung‐Min Kang Do‐Hee Kim Chenglong Jin Hee‐Chul Ahn Bong‐Jin Lee |
| author_facet | Sung‐Min Kang Do‐Hee Kim Chenglong Jin Hee‐Chul Ahn Bong‐Jin Lee |
| author_sort | Sung‐Min Kang |
| collection | DOAJ |
| description | Transcriptional regulator proteins are closely involved in essential survival strategies in bacteria. AcrR is a one‐component allosteric repressor of the genes associated with lipid transport and antibiotic resistance. When fatty acid ligands bind to the C‐terminal ligand‐binding cavity of AcrR, a conformational change in the N‐terminal operator‐binding region of AcrR is triggered, which releases the repressed DNA and initiates transcription. This paper focuses on the structural transition mechanism of AcrR of Mycobacterium tuberculosis upon DNA and ligand binding. AcrR loses its structural integrity upon ligand‐mediated structural alteration and bends toward the promoter DNA in a more compact form, initiating a rotational motion. Our functional characterization of AcrR and description of the ligand‐ and DNA‐recognition mechanism may facilitate the discovery of new therapies for tuberculosis. |
| format | Article |
| id | doaj-art-0bc95aa3dd404d97948eb4f5e1ee19d6 |
| institution | Kabale University |
| issn | 2211-5463 |
| language | English |
| publishDate | 2019-10-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj-art-0bc95aa3dd404d97948eb4f5e1ee19d62024-12-06T11:26:04ZengWileyFEBS Open Bio2211-54632019-10-019101713172510.1002/2211-5463.12710The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanismSung‐Min Kang0Do‐Hee Kim1Chenglong Jin2Hee‐Chul Ahn3Bong‐Jin Lee4The Research Institute of Pharmaceutical Sciences, College of Pharmacy Seoul National University Seoul KoreaThe Research Institute of Pharmaceutical Sciences, College of Pharmacy Seoul National University Seoul KoreaThe Research Institute of Pharmaceutical Sciences, College of Pharmacy Seoul National University Seoul KoreaDepartment of Pharmacy Dongguk University‐Seoul Ilsandong‐gu Goyang KoreaThe Research Institute of Pharmaceutical Sciences, College of Pharmacy Seoul National University Seoul KoreaTranscriptional regulator proteins are closely involved in essential survival strategies in bacteria. AcrR is a one‐component allosteric repressor of the genes associated with lipid transport and antibiotic resistance. When fatty acid ligands bind to the C‐terminal ligand‐binding cavity of AcrR, a conformational change in the N‐terminal operator‐binding region of AcrR is triggered, which releases the repressed DNA and initiates transcription. This paper focuses on the structural transition mechanism of AcrR of Mycobacterium tuberculosis upon DNA and ligand binding. AcrR loses its structural integrity upon ligand‐mediated structural alteration and bends toward the promoter DNA in a more compact form, initiating a rotational motion. Our functional characterization of AcrR and description of the ligand‐ and DNA‐recognition mechanism may facilitate the discovery of new therapies for tuberculosis.https://doi.org/10.1002/2211-5463.12710AcrRMycobacterium tuberculosistranscriptional regulatorX‐ray crystallography |
| spellingShingle | Sung‐Min Kang Do‐Hee Kim Chenglong Jin Hee‐Chul Ahn Bong‐Jin Lee The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism FEBS Open Bio AcrR Mycobacterium tuberculosis transcriptional regulator X‐ray crystallography |
| title | The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism |
| title_full | The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism |
| title_fullStr | The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism |
| title_full_unstemmed | The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism |
| title_short | The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one‐component transcriptional regulation mechanism |
| title_sort | crystal structure of acrr from mycobacterium tuberculosis reveals a one component transcriptional regulation mechanism |
| topic | AcrR Mycobacterium tuberculosis transcriptional regulator X‐ray crystallography |
| url | https://doi.org/10.1002/2211-5463.12710 |
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