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EC Number
Crystallization (Commentary)
1.3.3.16
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
1.3.3.16
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
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