7LZA

Activated form of VanR from S. coelicolor

7LZA の概要

• エントリーDOI: 10.2210/pdb7lza/pdb
• 関連するPDBエントリー: 7LZ9
• 分子名称: Putative two-component system response regulator, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: beryllium fluoride, antibiotic resistance, response regulator, transcription
• 由来する生物種: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25066.58

構造登録者

Maciunas, L.J.,Loll, P.J. (登録日: 2021-03-09, 公開日: 2021-07-14, 最終更新日: 2023-10-18)

主引用文献

Maciunas, L.J.,Porter, N.,Lee, P.J.,Gupta, K.,Loll, P.J.
Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.
Acta Crystallogr D Struct Biol, 77:1027-1039, 2021

PubMed Abstract: Vancomycin has historically been used as a last-resort treatment for serious bacterial infections. However, vancomycin resistance has become widespread in certain pathogens, presenting a serious threat to public health. Resistance to vancomycin is conferred by a suite of resistance genes, the expression of which is controlled by the VanR-VanS two-component system. VanR is the response regulator in this system; in the presence of vancomycin, VanR accepts a phosphoryl group from VanS, thereby activating VanR as a transcription factor and inducing expression of the resistance genes. This paper presents the X-ray crystal structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states at resolutions of 2.3 and 2.0 Å, respectively. Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein. This transition generates an interface that promotes dimerization of the receiver domain; dimerization in solution was verified using analytical ultracentrifugation. The inactive conformation of the protein does not appear intrinsically unable to bind DNA; rather, it is proposed that in the activated form DNA binding is enhanced by an avidity effect contributed by the receiver-domain dimerization.

PubMed: 34342276
DOI: 10.1107/S2059798321006288

実験手法

X-RAY DIFFRACTION (2.03 Å)