Summary for 9EBR
| Entry DOI | 10.2210/pdb9ebr/pdb |
| Descriptor | Probable transcription repressor NiaR, FE (II) ION, NICOTINIC ACID, ... (5 entities in total) |
| Functional Keywords | corepressor, regulatory protein, metalloprotein, dna binding protein |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 1 |
| Total formula weight | 19877.89 |
| Authors | Glasfeld, A.,Cheng, D.W.C.,Li, Y. (deposition date: 2024-11-13, release date: 2025-01-22, Last modification date: 2025-04-02) |
| Primary citation | 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 Cited by 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: 39899144DOI: 10.1007/s00775-025-02096-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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