9L8V

PyrN C-terminl domain in complex with L-glutamyl-sulfamoyl-adenosine (GSA)

This is a non-PDB format compatible entry.

Summary for 9L8V

• Entry DOI: 10.2210/pdb9l8v/pdb
• Descriptor: Methionine-tRNA ligase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ZINC ION, ... (5 entities in total)
• Functional Keywords: methionine biosynthesis streptomyces atp, ligase
• Biological source: Streptomyces candidus
• Total number of polymer chains: 4
• Total formula weight: 242607.95

Authors

Du, Y.L.,Zhao, G. (deposition date: 2024-12-28, release date: 2025-12-31, Last modification date: 2026-07-29)

Primary citation

Zhao, G.,Huang, H.,Li, Y.,Yang, J.,Guo, Y.Y.,Xu, L.,Wang, L.,Shi, J.,Wu, M.,Feng, Y.,Wang, B.,Zhang, Z.M.,Du, Y.L.
Structural and Mechanistic Insights into Bacterial Hydrazine Biosynthesis.
J.Am.Chem.Soc., 147:42984-42993, 2025

PubMed Abstract: Nitrogen-nitrogen (N-N) bond-containing motifs are prevalent in both clinical drugs and natural products. Bacterial hydrazine synthetases catalyze N-N bond formation by coupling an amino acid and a hydroxylamine via a distinctive -aminoacyl-hydroxylamine intermediate. Despite its wide occurrence, the structural and mechanistic basis of this process has remained elusive. Here, we report the first crystal structures of the -aminoacyl-hydroxylamine synthetase (aaHS) component of a bacterial hydrazine synthetase, captured in binary and ternary complexes with substrates and catalytic intermediates. These structures reveal the molecular determinants of substrate recognition and, together with biochemical and computational analyses, establish a detailed mechanistic framework for the hydrazine synthetase family. Leveraging these insights, we expanded hydrazine biosynthesis through the targeted discovery of novel hydrazine synthetases and implemented a chemoenzymatic synthesis strategy. This work provides fundamental insights into hydrazine synthetases and lays the groundwork for their rational engineering as versatile biocatalysts.

PubMed: 41191408
DOI: 10.1021/jacs.5c15949

Experimental method

X-RAY DIFFRACTION (2.23 Å)