Structural characterization of MAB_4123, a putative two-component flavin-dependent monooxygenase from the human pathogen Mycobacterium abscessus, suggests a role in the catabolic pathway of organosulfur compounds.

The single-component flavin-dependent tryptophan halogenase AetF converts tryptophan to 5,7-dibromotryptophan during the biosynthesis of the neurotoxin aetokthonotoxin. Crystal structures of AetF with the substrates tryptophan and 5-bromotryptophan show that a flip of the indole moiety of tryptophan positions first C5 and then C7 in the same location in the active site to facilitate two successive bromination reactions.

Methanobactins are post-translationally modified copper-binding peptides that have a number of potential environmental and biomedical applications. This report presents the crystal structure and preliminary biochemical characterization of the putative methanobactin biosynthesis protein MbnF.

The structure of human MICAL3 provides information about its mechanism.

p-Hydroxybenzoate hydroxylase (PobA) is a possible drug target to combat tetracycline resistance. Here, the 2.2 Å resolution structure of PobA from the pathogen Pseudomonas putida complexed with FAD is reported and is compared with those of PobA from P. aeruginosa and P. fluorescens.

The anthracycline biosynthetic enzyme DnmZ has been structurally characterized in ligand-free and thymidine diphosphate-bound forms.

Microcrystals of HpaB were formed while isolating integral membrane respiratory complexes from Thermus thermophilus. Further purification of the enzyme was achieved by repetitive crystallization. Subsequently, well shaped single crystals of the native enzyme that diffracted to 1.82 Å resolution were grown in sitting drops.

The flavin-dependent monooxygenase RebC has been crystallized by the hanging-drop vapour-diffusion method and initial X-ray diffraction analysis has been completed.

The high-resolution crystal structure of a Zonocerus variegatus flavin-dependent monooxygenase is reported at 1.6 Å resolution together with kinetic studies of structure-based protein variants in order to investigate significant differences in enzyme activity between isoforms.

Crystal structure analyses of the monooxygenase TetX in complex with tigecycline and minocycline support the observation that all clinically available tetracycline antibiotics can be inactivated by enzymatic hydroxylation. Molecular-dynamics simulations of dioxygen diffusion and experimental xenon-binding sites in TetX are compared with respect to putative dioxygen-binding cavities and dioxygen-diffusion pathways.