8JZD

Crystal structure of Escherichia coli NarJ in complex with the signal peptide of E. coli NarG

8JZD の概要

• エントリーDOI: 10.2210/pdb8jzd/pdb
• 分子名称: Nitrate reductase molybdenum cofactor assembly chaperone NarJ, Respiratory nitrate reductase 1 alpha chain (2 entities in total)
• 機能のキーワード: redox enzyme maturation protein, chaperone, narj subfamily, signal peptide
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47476.03

構造登録者

Song, W.S.,Kim, J.H.,Namgung, B.,Cho, H.Y.,Oh, H.B.,Yoon, S.I. (登録日: 2023-07-05, 公開日: 2024-05-15)

主引用文献

Song, W.S.,Kim, J.H.,Namgung, B.,Cho, H.Y.,Shin, H.,Oh, H.B.,Ha, N.C.,Yoon, S.I.
Complementary hydrophobic interaction of the redox enzyme maturation protein NarJ with the signal peptide of the respiratory nitrate reductase NarG.
Int.J.Biol.Macromol., 262:129620-129620, 2024

PubMed Abstract: In bacteria, NarJ plays an essential role as a redox enzyme maturation protein in the assembly of the nitrate reductase NarGHI by interacting with the N-terminal signal peptide of NarG to facilitate cofactor incorporation into NarG. The purpose of our research was to elucidate the exact mechanism of NarG signal peptide recognition by NarJ. We determined the structures of NarJ alone and in complex with the signal peptide of NarG via X-ray crystallography and verified the NarJ-NarG interaction through mutational, binding, and molecular dynamics simulation studies. NarJ adopts a curved α-helix bundle structure with a U-shaped hydrophobic groove on its concave side. This groove accommodates the signal peptide of NarG via a dual binding mode in which the left and right parts of the NarJ groove each interact with two consecutive hydrophobic residues from the N- and C-terminal regions of the NarG signal peptide, respectively, through shape and chemical complementarity. This binding is accompanied by unwinding of the helical structure of the NarG signal peptide and by stabilization of the NarG-binding loop of NarJ. We conclude that NarJ recognizes the NarG signal peptide through a complementary hydrophobic interaction mechanism that mediates a structural rearrangement.

PubMed: 38262549
DOI: 10.1016/j.ijbiomac.2024.129620

実験手法

X-RAY DIFFRACTION (2.45 Å)