9EBR

The structure of NiaR from Thermotoga maritima bound to nicotinic acid

「9BUL」から置き換えられました

9EBR の概要

• エントリーDOI: 10.2210/pdb9ebr/pdb
• 分子名称: Probable transcription repressor NiaR, FE (II) ION, NICOTINIC ACID, ... (5 entities in total)
• 機能のキーワード: corepressor, regulatory protein, metalloprotein, dna binding protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19877.89

構造登録者

Glasfeld, A.,Cheng, D.W.C.,Li, Y. (登録日: 2024-11-13, 公開日: 2025-01-22, 最終更新日: 2025-04-02)

主引用文献

Cheng, W.C.D.,Li, Y.,Nakashima, M.,Moenne-Loccoz, P.,Rush, K.W.,Glasfeld, A.
The activation of the metal-containing regulatory protein NiaR from Thermotoga maritima by its effector, nicotinic acid.
J.Biol.Inorg.Chem., 30:169-179, 2025

PubMed Abstract: NiaR is a regulatory protein that represses the expression of proteins involved in the de novo biosynthesis and uptake of nicotinic acid (NA), with NA acting as a co-repressor. The previously published structure of NiaR from Thermotoga maritima (TmNiaR) identified it as a functional homodimer containing a transition metal ion in a suspected NA-binding pocket. Here, we present the crystal structure of NA bound to the iron-metalated form of TmNiaR. Supported by spectroscopic and solution studies, this structure shows that NA binds to a protein-bound ferrous ion via its ring nitrogen. In addition, the carboxylate group on NA interacts with Tyr108 from the dyad-related subunit, repositioning the likely DNA-binding domains of the dimer to promote high-affinity interactions with DNA operators. The specificity of TmNiaR for NA can be explained by the hydrogen bonding scheme within the NA-binding pocket.

PubMed: 39899144
DOI: 10.1007/s00775-025-02096-y

実験手法

X-RAY DIFFRACTION (2.3 Å)