5JTF

Crystal structure of ArsN N-acetyltransferase from Pseudomonas putida KT2440

Summary for 5JTF

• Entry DOI: 10.2210/pdb5jtf/pdb
• Descriptor: Putative Phosphinothricin N-acetyltransferase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: n-acetyltransferase, pseudomonas putida, transferase
• Biological source: Pseudomonas putida
• Total number of polymer chains: 2
• Total formula weight: 46884.76

Authors

Venkadesh, S.,Dheeman, D.S.,Kandavelu, P.,Rosen, B.P. (deposition date: 2016-05-09, release date: 2017-05-17, Last modification date: 2023-09-27)

Primary citation

Nadar, V.S.,Chen, J.,Dheeman, D.S.,Galvan, A.E.,Yoshinaga-Sakurai, K.,Kandavelu, P.,Sankaran, B.,Kuramata, M.,Ishikawa, S.,Rosen, B.P.,Yoshinaga, M.
Arsinothricin, an arsenic-containing non-proteinogenic amino acid analog of glutamate, is a broad-spectrum antibiotic.
Commun Biol, 2:131-131, 2019

PubMed Abstract: The emergence and spread of antimicrobial resistance highlights the urgent need for new antibiotics. Organoarsenicals have been used as antimicrobials since Paul Ehrlich's salvarsan. Recently a soil bacterium was shown to produce the organoarsenical arsinothricin. We demonstrate that arsinothricin, a non-proteinogenic analog of glutamate that inhibits glutamine synthetase, is an effective broad-spectrum antibiotic against both Gram-positive and Gram-negative bacteria, suggesting that bacteria have evolved the ability to utilize the pervasive environmental toxic metalloid arsenic to produce a potent antimicrobial. With every new antibiotic, resistance inevitably arises. The gene, widely distributed in bacterial arsenic resistance () operons, selectively confers resistance to arsinothricin by acetylation of the α-amino group. Crystal structures of ArsN1 -acetyltransferase, with or without arsinothricin, shed light on the mechanism of its substrate selectivity. These findings have the potential for development of a new class of organoarsenical antimicrobials and ArsN1 inhibitors.

PubMed: 30993215
DOI: 10.1038/s42003-019-0365-y

Experimental method

X-RAY DIFFRACTION (2.156 Å)