Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics

The siderophore biosynthetic enzyme A (SidA) ornithine hydroxylase from Aspergillus fumigatus is a fungal disease drug target involved in the production of hydroxamate-containing siderophores, which are used by the pathogen to sequester iron. SidA is an N-monooxygenase that catalyzes the NADPH-depen...

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Udgivet i:J Biol Chem
Main Authors: Campbell, Ashley C., Stiers, Kyle M., Martin Del Campo, Julia S., Mehra-Chaudhary, Ritcha, Sobrado, Pablo, Tanner, John J.
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2020
Fag:
Protein Structure and Folding
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC7504930/
https://ncbi.nlm.nih.gov/pubmed/32723870
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA120.014750
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