6FI9

Crystal Structure of a zinc-responsive MarR family member, Lactococcus lactis ZitR

6FI9 の概要

• エントリーDOI: 10.2210/pdb6fi9/pdb
• 分子名称: Transcriptional regulator ZitR, ZINC ION (2 entities in total)
• 機能のキーワード: zinc transport regulator, adhesin competence regulator, multiple antibiotic resistance regulator, zinc responsive repressor, winged helix-turn-helix dna binding domain, gene regulation
• 由来する生物種: Lactococcus lactis subsp. cremoris (strain MG1363)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 131507.09

構造登録者

Varela, P.F.,Legrand, P. (登録日: 2018-01-17, 公開日: 2019-02-20, 最終更新日: 2024-05-08)

主引用文献

Varela, P.F.,Velours, C.,Aumont-Nicaise, M.,Pineau, B.,Legrand, P.,Poquet, I.
Biophysical and structural characterization of a zinc-responsive repressor of the MarR superfamily.
PLoS ONE, 14:e0210123-e0210123, 2019

PubMed Abstract: The uptake of zinc, which is vital in trace amounts, is tightly controlled in bacteria. For this control, bacteria of the Streptococcaceae group use a Zn(II)-binding repressor named ZitR in lactococci and AdcR in streptococci, while other bacteria use a Zur protein of the Ferric uptake regulator (Fur) superfamily. ZitR and AdcR proteins, characterized by a winged helix-turn-helix DNA-binding domain, belong to the multiple antibiotic resistance (MarR) superfamily, where they form a specific group of metallo-regulators. Here, one such Zn(II)-responsive repressor, ZitR of Lactococcus lactis subspecies cremoris strain MG1363, is characterized. Size Exclusion Chromatography-coupled to Multi Angle Light Scattering, Circular Dichroism and Isothermal Titration Calorimetry show that purified ZitR is a stable dimer complexed to Zn(II), which is able to bind its two palindromic operator sites on DNA fragments. The crystal structure of ZitR holo-form (Zn(II)4-ZitR2), has been determined at 2.8 Å resolution. ZitR is the fourth member of the MarR metallo-regulator subgroup whose structure has been determined. The folding of ZitR/AdcR metallo-proteins is highly conserved between both subspecies (cremoris or lactis) in the Lactococcus lactis species and between species (Lactococcus lactis and Streptococcus pneumoniae or pyogenes) in the Streptococcaceae group. It is also similar to the folding of other MarR members, especially in the DNA-binding domain. Our study contributes to better understand the biochemical and structural properties of metallo-regulators in the MarR superfamily.

PubMed: 30753183
DOI: 10.1371/journal.pone.0210123

実験手法

X-RAY DIFFRACTION (2.8 Å)