5eri
MarR Protein from Peptoclostridium difficile DA00132MarR Protein from Peptoclostridium difficile DA00132
Structural highlights
FunctionPublication Abstract from PubMedRegulators 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 (MarRC.difficile) was subcloned and crystallized for the first time. MarRC.difficile 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 MarRC.difficile has been solved at 2.3 A resolution. The crystal belonged to the monoclinic space group P43212, with unit-cell parameters a = b = 66.569, c = 83.654 A. The structure reported reveals MarRC.difficile to be a dimer, with each subunit consisting of six alpha-helices and three antiparallel beta-hairpins. MarRC.difficile shows high structural similarity to the MarR proteins from E. coli and Staphylococcus aureus, indicating that MarRC.difficile might be a DNA-binding protein. Crystal structure of the multiple antibiotic resistance regulator MarR from Clostridium difficile.,Peng JW, Yuan H, Tan XS Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):363-368. doi:, 10.1107/S2053230X1700766X. Epub 2017 May 31. PMID:28580925[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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