7TCR
Methanobactin biosynthetic protein complex of MbnB and MbnC from Methylosinus trichosporium OB3b at 2.62 Angstrom resolution
Summary for 7TCR
Entry DOI | 10.2210/pdb7tcr/pdb |
Related | 7TCU 7TCW 7TCX |
Descriptor | Methanobactin biosynthesis cassette protein MbnB, Methanobactin biosynthesis cassette protein MbnC, FE (III) ION, ... (5 entities in total) |
Functional Keywords | metalloprotein, natural product biosynthetic protein, complex, biosynthetic protein |
Biological source | Methylosinus trichosporium OB3b More |
Total number of polymer chains | 4 |
Total formula weight | 107839.08 |
Authors | Park, Y.,Reyes, R.M.,Rosenzweig, A.C. (deposition date: 2021-12-28, release date: 2022-03-23, Last modification date: 2024-02-28) |
Primary citation | Park, Y.J.,Jodts, R.J.,Slater, J.W.,Reyes, R.M.,Winton, V.J.,Montaser, R.A.,Thomas, P.M.,Dowdle, W.B.,Ruiz, A.,Kelleher, N.L.,Bollinger Jr., J.M.,Krebs, C.,Hoffman, B.M.,Rosenzweig, A.C. A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis. Proc.Natl.Acad.Sci.USA, 119:e2123566119-e2123566119, 2022 Cited by PubMed Abstract: SignificanceMethanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper overload. The paired oxazolone-thioamide bidentate ligands of methanobactins are generated from cysteine residues in a precursor peptide, MbnA, by the MbnBC enzyme complex. MbnBC activity depends on the presence of iron and oxygen, but the catalytically active form has not been identified. Here, we provide evidence that a dinuclear Fe(II)Fe(III) center in MbnB, which is the only representative of a >13,000-member protein family to be characterized, is responsible for this reaction. These findings expand the known roles of diiron enzymes in biology and set the stage for mechanistic understanding, and ultimately engineering, of the MbnBC biosynthetic complex. PubMed: 35320042DOI: 10.1073/pnas.2123566119 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.62 Å) |
Structure validation
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