5ERI

MarR Protein from Peptoclostridium difficile DA00132

5ERI の概要

• エントリーDOI: 10.2210/pdb5eri/pdb
• 分子名称: MarR family transcriptional regulator (2 entities in total)
• 機能のキーワード: peptoclostridium difficile, marr, transcription factor, dna-binding, transcription
• 由来する生物種: Peptoclostridium difficile
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19549.44

構造登録者

Yuan, H.,Peng, J.W.,Tan, X.S. (登録日: 2015-11-14, 公開日: 2016-11-16, 最終更新日: 2023-11-08)

主引用文献

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

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: 28580925
DOI: 10.1107/S2053230X1700766X

実験手法

X-RAY DIFFRACTION (2.3 Å)