9BXA

Structure of Mnx H340A complex from Bacillus sp. PL-12

9BXA の概要

• エントリーDOI: 10.2210/pdb9bxa/pdb
• EMDBエントリー: 45001
• 分子名称: MnxG, MnxE, MnxF (3 entities in total)
• 機能のキーワード: complex, multicopper oxidase, manganese biomineralization, metal transport
• 由来する生物種: Bacillus sp. (in: firmicutes); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 210976.58

構造登録者

Novikova, I.V.,Evans, J.E. (登録日: 2024-05-22, 公開日: 2024-08-07, 最終更新日: 2024-10-30)

主引用文献

Novikova, I.V.,Soldatova, A.V.,Moser, T.H.,Thibert, S.M.,Romano, C.A.,Zhou, M.,Tebo, B.M.,Evans, J.E.,Spiro, T.G.
Cryo-EM Structure of the Mnx Protein Complex Reveals a Tunnel Framework for the Mechanism of Manganese Biomineralization.
J.Am.Chem.Soc., 146:22950-22958, 2024

PubMed Abstract: The global manganese cycle relies on microbes to oxidize soluble Mn(II) to insoluble Mn(IV) oxides. Some microbes require peroxide or superoxide as oxidants, but others can use O directly, via multicopper oxidase (MCO) enzymes. One of these, MnxG from strain PL-12, was isolated in tight association with small accessory proteins, MnxE and MnxF. The protein complex, called Mnx, has eluded crystallization efforts, but we now report the 3D structure of a point mutant using cryo-EM single particle analysis, cross-linking mass spectrometry, and AlphaFold Multimer prediction. The β-sheet-rich complex features MnxG enzyme, capped by a heterohexameric ring of alternating MnxE and MnxF subunits, and a tunnel that runs through MnxG and its MnxEF cap. The tunnel dimensions and charges can accommodate the mechanistically inferred binuclear manganese intermediates. Comparison with the Fe(II)-oxidizing MCO, ceruloplasmin, identifies likely coordinating groups for the Mn(II) substrate, at the entrance to the tunnel. Thus, the 3D structure provides a rationale for the established manganese oxidase mechanism, and a platform for further experiments to elucidate mechanistic details of manganese biomineralization.

PubMed: 39056168
DOI: 10.1021/jacs.3c06537

実験手法

ELECTRON MICROSCOPY (3.37 Å)