Complete genome sequence of Thermomonospora curvata type strain (B9).
Substrates control multimerization and activation of the multi-domain ATPase motor of type VII secretion.
Copper is a cofactor of the formylglycine-generating enzyme.
In vitro reconstitution of formylglycine-generating enzymes requires copper(I).
Structural basis for copper-oxygen mediated C-H bond activation by the formylglycine-generating enzyme.
The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site.
Identification of Surface-Exposed Protein Radicals and A Substrate Oxidation Site in A-Class Dye-Decolorizing Peroxidase from Thermomonospora curvata.
The ArsI C-As lyase: Elucidating the catalytic mechanism of degradation of organoarsenicals.
A Key Glycine in Bacterial Steroid-Degrading Acyl-CoA Dehydrogenases Allows Flavin-Ring Repositioning and Modulates Substrate Side Chain Specificity.
Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.
Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen.
Discovery of the Lanthipeptide Curvocidinand Structural Insights into its Trifunctional Synthetase CuvL.
Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL.