7DVN
Crystal structure of a MarR family protein in complex with a lipid-like effector molecule from the psychrophilic bacterium Paenisporosarcina sp. TG-14
Summary for 7DVN
| Entry DOI | 10.2210/pdb7dvn/pdb |
| Descriptor | MarR family transcriptional regulator, PALMITIC ACID (3 entities in total) |
| Functional Keywords | transcription regulator dna-binding complex lipid-like effector marr family, dna binding protein |
| Biological source | Paenisporosarcina sp. TG-14 |
| Total number of polymer chains | 1 |
| Total formula weight | 17194.24 |
| Authors | |
| Primary citation | Hwang, J.,Park, S.H.,Lee, C.W.,Do, H.,Shin, S.C.,Kim, H.W.,Lee, S.G.,Park, H.H.,Kwon, S.,Lee, J.H. Crystal structure of a MarR family protein from the psychrophilic bacterium Paenisporosarcina sp. TG-14 in complex with a lipid-like molecule. Iucrj, 8:842-852, 2021 Cited by PubMed Abstract: 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 sp. TG-14, which was isolated from sediment-laden basal ice in Antarctica. In this study, the crystal structure of the MarR protein from sp. TG-14 (MarR) 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 MarR 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 MarR binds to cognate DNA, where MarR is known to recognize two putative binding sites depending on its molar concentration, indicating that MarR 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. PubMed: 34584745DOI: 10.1107/S2052252521005704 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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