The biosynthesis of methanobactin
| Autor: | Grace E. Kenney, Steven C. Almo, Anthony S. Gizzi, Paul M. Thomas, Caroline J. DeHart, J. Martin Bollinger, Amy C. Rosenzweig, Laura M. K. Dassama, Monica Sadek, Neil L. Kelleher, Owen S. Skinner, Soo Y. Ro, Maria-Eirini Pandelia, Xiao Zhu, Ryan J. Martinie, Carsten Krebs, Peng Gao, Luis F. Schachner |
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| Rok vydání: | 2018 |
| Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine Peptide Bacterial genome size Ligands 010402 general chemistry 01 natural sciences Article Oxazolone 03 medical and health sciences chemistry.chemical_compound Protein structure Biosynthesis Amino Acid Sequence Peptide sequence chemistry.chemical_classification Multidisciplinary Chemistry Imidazoles Methanobactin Methylosinus trichosporium 0104 chemical sciences Oxygen 030104 developmental biology Enzyme Biochemistry Protein Multimerization Oligopeptides Oxidation-Reduction Protein Processing Post-Translational Copper Genome Bacterial |
| Zdroj: | Science. 359:1411-1416 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.aap9437 |
| Popis: | Using iron to generate a copper ligandMany microbial enzymes are metal-dependent, and the microbe must acquire scarce metals from the environment. Microbes that use methane as a carbon source have a copper-dependent enzyme that oxidizes the methane. Peptides known as methanobactins (Mbns) acquire copper by using a pair of ligands comprising a nitrogen-containing ring and an adjacent thioamide. Kenneyet al.describe the biosynthetic machinery that adds the copper-binding groups to a precursor peptide. This involves a complex of two homologs: MbnB, a member of a functionally uncharacterized protein family that includes a diiron cluster, and MbnC, which is even less well characterized. The iron cofactor is required for ligand synthesis. MbnB and MbnC homologs are encoded in many genomes, suggesting that they may have roles beyond Mbn biosynthesis.Science, this issue p.1411 |
| Databáze: | OpenAIRE |
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