7VVX

MmtN-SAH-Met complex

7VVX の概要

• エントリーDOI: 10.2210/pdb7vvx/pdb
• 分子名称: SAM-dependent methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, METHIONINE, ... (5 entities in total)
• 機能のキーワード: sam-dependent, methyltransferase, complex, rossmann-like, transferase
• 由来する生物種: Roseovarius indicus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 99759.47

構造登録者

Zhang, Y.Z.,Peng, M.,Li, C.Y. (登録日: 2021-11-09, 公開日: 2022-04-20, 最終更新日: 2024-05-29)

主引用文献

Peng, M.,Li, C.Y.,Chen, X.L.,Williams, B.T.,Li, K.,Gao, Y.N.,Wang, P.,Wang, N.,Gao, C.,Zhang, S.,Schoelmerich, M.C.,Banfield, J.F.,Miller, J.B.,Le Brun, N.E.,Todd, J.D.,Zhang, Y.Z.
Insights into methionine S-methylation in diverse organisms.
Nat Commun, 13:2947-2947, 2022

PubMed Abstract: Dimethylsulfoniopropionate (DMSP) is an important marine anti-stress compound, with key roles in global nutrient cycling, chemotaxis and, potentially, climate regulation. Recently, diverse marine Actinobacteria, α- and γ-proteobacteria were shown to initiate DMSP synthesis via the methionine (Met) S-methyltransferase enzyme (MmtN), generating S-methyl-Met (SMM). Here we characterize a roseobacterial MmtN, providing structural and mechanistic insights into this DMSP synthesis enzyme. We propose that MmtN uses the proximity and desolvation mechanism for Met S-methylation with two adjacent MmtN monomers comprising the Met binding site. We also identify diverse functional MmtN enzymes in potentially symbiotic archaeal Candidatus Woesearchaeota and Candidate Phyla Radiation (CPR) bacteria, and the animalcule Adineta steineri, not anticipated to produce SMM and/or DMSP. These diverse MmtN enzymes, alongside the larger plant MMT enzyme with an N-terminus homologous to MmtN, likely utilize the same proximity and desolvation mechanism. This study provides important insights into the catalytic mechanism of SMM and/or DMSP production, and proposes roles for these compounds in secondary metabolite production, and SMM cycling in diverse organisms and environments.

PubMed: 35618717
DOI: 10.1038/s41467-022-30491-5

実験手法

X-RAY DIFFRACTION (2.51 Å)