7TCU

Methanobactin biosynthetic protein complex of MbnB and MbnC from Methylosinus trichosporium OB3b at 2.31 Angstrom resolution

7TCU の概要

• エントリーDOI: 10.2210/pdb7tcu/pdb
• 分子名称: Methanobactin biosynthesis cassette protein MbnB, Methanobactin biosynthesis cassette protein MbnC, FE (III) ION, ... (5 entities in total)
• 機能のキーワード: metalloprotein, natural product biosynthetic protein, complex, biosynthetic protein
• 由来する生物種: Methylosinus trichosporium OB3b; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 107646.95

構造登録者

Park, Y.,Reyes, R.M.,Rosenzweig, A.C. (登録日: 2021-12-28, 公開日: 2022-03-23, 最終更新日: 2023-10-18)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.31 Å)