7XCN

Crystal structure of the MttB-MttC complex at 2.7 A resolution

7XCN の概要

• エントリーDOI: 10.2210/pdb7xcn/pdb
• 分子名称: Trimethylamine methyltransferase, Trimethylamine methyltransferase corrinoid protein, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: pyrrolysine, trimethylamine, methyltransferase, corrinoid protein, transferase
• 由来する生物種: Methanosarcina barkeri MS; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 480854.44

構造登録者

Li, J.,Chan, M.K. (登録日: 2022-03-24, 公開日: 2023-01-18, 最終更新日: 2023-11-29)

主引用文献

Li, J.,Kang, P.T.,Jiang, R.,Lee, J.Y.,Soares, J.A.,Krzycki, J.A.,Chan, M.K.
Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.
Commun Biol, 6:54-54, 2023

PubMed Abstract: The 22nd genetically encoded amino acid, pyrrolysine, plays a unique role in the key step in the growth of methanogens on mono-, di-, and tri-methylamines by activating the methyl group of these substrates for transfer to a corrinoid cofactor. Previous crystal structures of the Methanosarcina barkeri monomethylamine methyltransferase elucidated the structure of pyrrolysine and provide insight into its role in monomethylamine activation. Herein, we report the second structure of a pyrrolysine-containing protein, the M. barkeri trimethylamine methyltransferase MttB, and its structure bound to sulfite, a substrate analog of trimethylamine. We also report the structure of MttB in complex with its cognate corrinoid protein MttC, which specifically receives the methyl group from the pyrrolysine-activated trimethylamine substrate during methanogenesis. Together these structures provide key insights into the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC.

PubMed: 36646841
DOI: 10.1038/s42003-022-04397-3

実験手法

X-RAY DIFFRACTION (2.7 Å)