4ZMS

Structure of the full-length response regulator spr1814 in complex with a phosphate analogue and B3C

4ZMS の概要

• エントリーDOI: 10.2210/pdb4zms/pdb
• 関連するPDBエントリー: 4zmr
• 分子名称: Response regulator, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• 機能のキーワード: response regulator, dna binding protein
• 由来する生物種: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46765.69

構造登録者

Chi, Y.M.,Park, A. (登録日: 2015-05-04, 公開日: 2016-04-27, 最終更新日: 2024-03-20)

主引用文献

Park, A.K.,Lee, J.H.,Chi, Y.M.,Park, H.
Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region
Biochem.Biophys.Res.Commun., 473:625-629, 2016

PubMed Abstract: Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3(-)) was determined at 2.0 Å. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.

PubMed: 27038544
DOI: 10.1016/j.bbrc.2016.03.144

実験手法

X-RAY DIFFRACTION (1.9 Å)