9BQ0
Complex structure of protein crystal of Tri17 with ATP
Summary for 9BQ0
| Entry DOI | 10.2210/pdb9bq0/pdb |
| Related | 8TF7 |
| Descriptor | AMP-binding protein, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | acyl-coa ligase, amp-binding domain, n-n bond formation, apo structure, ligase |
| Biological source | Streptomyces tsukubensis |
| Total number of polymer chains | 4 |
| Total formula weight | 248401.10 |
| Authors | |
| Primary citation | Del Rio Flores, A.,Zhai, R.,Kastner, D.W.,Seshadri, K.,Yang, S.,De Matias, K.,Shen, Y.,Cai, W.,Narayanamoorthy, M.,Do, N.B.,Xue, Z.,Marzooqi, D.A.,Kulik, H.J.,Zhang, W. Enzymatic synthesis of azide by a promiscuous N-nitrosylase. Nat.Chem., 2024 Cited by PubMed Abstract: Azides are energy-rich compounds with diverse representation in a broad range of scientific disciplines, including material science, synthetic chemistry, pharmaceutical science and chemical biology. Despite ubiquitous usage of the azido group, the underlying biosynthetic pathways for its formation remain largely unknown. Here we report the characterization of an enzymatic route for de novo azide construction. We demonstrate that Tri17, a promiscuous ATP- and nitrite-dependent enzyme, catalyses organic azide synthesis through sequential N-nitrosation and dehydration of aryl hydrazines. Through biochemical, structural and computational analyses, we further propose a plausible molecular mechanism for azide synthesis that sets the stage for future biocatalytic applications and biosynthetic pathway engineering. PubMed: 39333393DOI: 10.1038/s41557-024-01646-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
