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7TCR

Methanobactin biosynthetic protein complex of MbnB and MbnC from Methylosinus trichosporium OB3b at 2.62 Angstrom resolution

Summary for 7TCR
Entry DOI10.2210/pdb7tcr/pdb
Related7TCU 7TCW 7TCX
DescriptorMethanobactin biosynthesis cassette protein MbnB, Methanobactin biosynthesis cassette protein MbnC, FE (III) ION, ... (5 entities in total)
Functional Keywordsmetalloprotein, natural product biosynthetic protein, complex, biosynthetic protein
Biological sourceMethylosinus trichosporium OB3b
More
Total number of polymer chains4
Total formula weight107839.08
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 citationPark, 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: 35320042
DOI: 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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