5ERI
MarR Protein from Peptoclostridium difficile DA00132
Summary for 5ERI
| Entry DOI | 10.2210/pdb5eri/pdb |
| Descriptor | MarR family transcriptional regulator (2 entities in total) |
| Functional Keywords | peptoclostridium difficile, marr, transcription factor, dna-binding, transcription |
| Biological source | Peptoclostridium difficile |
| Total number of polymer chains | 1 |
| Total formula weight | 19549.44 |
| Authors | Yuan, H.,Peng, J.W.,Tan, X.S. (deposition date: 2015-11-14, release date: 2016-11-16, Last modification date: 2023-11-08) |
| Primary citation | Peng, J.W.,Yuan, H.,Tan, X.S. Crystal structure of the multiple antibiotic resistance regulator MarR from Clostridium difficile. Acta Crystallogr.,Sect.F, 73:363-368, 2017 Cited by PubMed Abstract: Regulators of multiple antibiotic resistance (MarRs) are key players against toxins in prokaryotes. MarR homologues have been identified in many bacterial and archaeal species which pose daunting antibiotic resistance issues that threaten public health. The continuous prevalence of Clostridium difficile infection (CDI) throughout the world is associated with the abuse of antibiotics, and antibiotic treatments of CDI have limited effect. In the genome of C. difficile strain 630, the marR gene (ID 4913953) encodes a MarR protein. Here, MarR from C. difficile (MarR) was subcloned and crystallized for the first time. MarR was successfully expressed in Escherichia coli in a soluble form and was purified to near-homogeneity (>95%) by a two-step purification protocol. The structure of MarR has been solved at 2.3 Å resolution. The crystal belonged to the monoclinic space group P422, with unit-cell parameters a = b = 66.569, c = 83.654 Å. The structure reported reveals MarR to be a dimer, with each subunit consisting of six α-helices and three antiparallel β-hairpins. MarR shows high structural similarity to the MarR proteins from E. coli and Staphylococcus aureus, indicating that MarR might be a DNA-binding protein. PubMed: 28580925DOI: 10.1107/S2053230X1700766X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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