9bq0 | pdb_00009bq0

Complex structure of protein crystal of Tri17 with ATP

spinqualitylabelsall models 9bq0, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bq0 is a 4 chain structure with sequence from Streptomyces tsukubensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Enzymatic synthesis of azide by a promiscuous N-nitrosylase.,Del Rio Flores A, Zhai R, Kastner DW, Seshadri K, Yang S, De Matias K, Shen Y, Cai W, Narayanamoorthy M, Do NB, Xue Z, Marzooqi DA, Kulik HJ, Zhang W Nat Chem. 2024 Sep 27. doi: 10.1038/s41557-024-01646-2. PMID:39333393 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA