5YHZ

Structure of Lactococcus lactis ZitR, E41A mutant

5YHZ の概要

• エントリーDOI: 10.2210/pdb5yhz/pdb
• 関連するPDBエントリー: 5YHX 5YHY 5YI0 5YI1 5YI2 5YI3
• 分子名称: Zinc transport transcriptional regulator, ZINC ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: zinc binding protein, marr family, winged helix-turn-helix, transcriptional regulator, metal binding protein
• 由来する生物種: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16819.89

構造登録者

Song, Y.,Liu, H.,Zhu, R.,Yi, C.,Chen, P. (登録日: 2017-10-01, 公開日: 2017-12-06, 最終更新日: 2023-11-22)

主引用文献

Zhu, R.,Song, Y.,Liu, H.,Yang, Y.,Wang, S.,Yi, C.,Chen, P.R.
Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation.
Proc.Natl.Acad.Sci.USA, 114:13661-13666, 2017

PubMed Abstract: Metalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR's high-affinity zinc site (site 1) switches from Nε2 to Nδ1 upon Zn(II) binding to its low-affinity zinc site (site 2), which facilitates ZitR's conversion from the nonoptimal to the optimal DNA-binding conformation. This histidine switch-mediated cooperation between site 1 and site 2 enables ZitR to adjust its DNA-binding affinity in response to a broad range of zinc fluctuation, which may allow the fine tuning of transcriptional regulation.

PubMed: 29229866
DOI: 10.1073/pnas.1708563115

実験手法

X-RAY DIFFRACTION (1.9 Å)