8TF7

Apo structure of protein crystal of Tri17

Summary for 8TF7

• Entry DOI: 10.2210/pdb8tf7/pdb
• Descriptor: AMP-binding protein (2 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: 2
• Total formula weight: 123757.98

Authors

Zhai, R.,Zhang, W. (deposition date: 2023-07-09, release date: 2024-07-10, Last modification date: 2024-10-09)

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

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: 39333393
DOI: 10.1038/s41557-024-01646-2

Experimental method

X-RAY DIFFRACTION (2.45 Å)