5ZU0

Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA

5ZU0 の概要

• エントリーDOI: 10.2210/pdb5zu0/pdb
• 関連するPDBエントリー: 5ZTZ
• 分子名称: Protein arginine methyltransferase NDUFAF7 homolog, mitochondrial, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: mida, mitochondrial complex i, sam, sah, protein arginine methyl transferase, transferase
• 由来する生物種: Dictyostelium discoideum (Slime mold)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 143490.80

構造登録者

Arold, S.T.,Swaminathan, K.,Hameed, U.F.S. (登録日: 2018-05-05, 公開日: 2018-08-22, 最終更新日: 2024-10-16)

主引用文献

Shahul Hameed, U.F.S.,Sanislav, O.,Lay, S.T.,Annesley, S.J.,Jobichen, C.,Fisher, P.R.,Swaminathan, K.,Arold, S.T.
Proteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA.
Cell Rep, 24:1996-2004, 2018

PubMed Abstract: The human protein arginine methyltransferase NDUFAF7 controls the assembly of the ∼1-MDa mitochondrial complex I (CI; the NADH ubiquinone oxidoreductase) by methylating its subunit NDUFS2. We determined crystal structures of MidA, the Dictyostelium ortholog of NDUFAF7. The MidA catalytic core domain resembles other eukaryotic methyltransferases. However, three large core loops assemble into a regulatory domain that is likely to control ligand selection. Binding of MidA to NDUFS2 is weakened by methylation, suggesting a mechanism for methylation-controlled substrate release. Structural and bioinformatic analyses support that MidA and NDUFAF7 and their role in CI assembly are conserved from bacteria to humans, implying that protein methylation already existed in proteobacteria. In vivo studies confirmed the critical role of the MidA methyltransferase activity for CI assembly, growth, and phototaxis of Dictyostelium. Collectively, our data elucidate the origin of protein arginine methylation and its use by MidA/NDUFAF7 to regulate CI assembly.

PubMed: 30134162
DOI: 10.1016/j.celrep.2018.07.075

実験手法

X-RAY DIFFRACTION (2.76 Å)