1.3.3.16: oxazoline dehydrogenase

This is an abbreviated version!
For detailed information about oxazoline dehydrogenase, go to the full flat file.

Reaction

a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
+
O2
=
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole
+
H2O2

Synonyms

artG, azoline oxidase, Cyan7425_0520, cyanobactin oxidase, lynG, MbcC, mcaG, McbB, McbC, McbD, microcin B17 synthase, microcin B17-processing protein McbC, PatG, tenG, ThcOx, thiazoline oxidase, thiazoline oxidase/subtilisin-like protease

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.16 oxazoline dehydrogenase

Crystallization

Crystallization on EC 1.3.3.16 - oxazoline dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 3.15 A resolution, space group P412121 with two molecules found in the asymmetric unit. The structure is composed of a novel domain and an FMN nitroreductase domain. The N-terminal domain contains a portion (residues 7-86) which possesses the same fold as the leader binding domain of TruD, the so-called peptide-clamp domain. The C-terminal domain (residues 323-469) contains the FMN molecule and has a high degree of homology to the putative nitroreductase from Anabaena variabilis
structures of synthetase McbBCD reveal an octameric B4C2D2 complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer