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May 2023 issue
Cover illustration: The asymetric unit of MbnF: an NAPDPH-dependent flavin monoxygenase from Methylocystis strain SB2 [Stewart et al. (2023), Acta Cryst. F79, 111–118]. Methanobactins are peptides produced by methanotrophs for copper acquisition. Although the exact biosynthetic pathway of methanobactin formation is not fully understood, MbnF is a protein associated with a methanobactin gene cluster. In this report, structural and functional studies of MbnF are used to gain insight into methanobactin biosynthesis.
research communications
The crystal structure of the engineered endolysin mtEC340M was determined at 2.4 Å resolution.
PDB reference: mtEC340M, 8hp8
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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.
PDB reference: MbnF, 8fhj
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Apo and acarbose-complex structures of the catalytic domain of GtfB from Streptococcus mutans and the truncated structure of the catalytic domain of GtfD are described.
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.
PDB reference: MAB_4123, 8cda
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