7OEY

Neisseria gonnorhoeae variant E93Q at 1.35 angstrom resolution

7OEY の概要

• エントリーDOI: 10.2210/pdb7oey/pdb
• 分子名称: Transaldolase, SUCCINIC ACID, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: transferase, sugar metabolism, post-translational modification
• 由来する生物種: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75762.85

構造登録者

Rabe von Pappenheim, F.,Wensien, M.,Tittmann, K. (登録日: 2021-05-04, 公開日: 2022-02-02, 最終更新日: 2024-11-13)

主引用文献

Rabe von Pappenheim, F.,Wensien, M.,Ye, J.,Uranga, J.,Irisarri, I.,de Vries, J.,Funk, L.M.,Mata, R.A.,Tittmann, K.
Widespread occurrence of covalent lysine-cysteine redox switches in proteins.
Nat.Chem.Biol., 18:368-375, 2022

PubMed Abstract: We recently reported the discovery of a lysine-cysteine redox switch in proteins with a covalent nitrogen-oxygen-sulfur (NOS) bridge. Here, a systematic survey of the whole protein structure database discloses that NOS bridges are ubiquitous redox switches in proteins of all domains of life and are found in diverse structural motifs and chemical variants. In several instances, lysines are observed in simultaneous linkage with two cysteines, forming a sulfur-oxygen-nitrogen-oxygen-sulfur (SONOS) bridge with a trivalent nitrogen, which constitutes an unusual native branching cross-link. In many proteins, the NOS switch contains a functionally essential lysine with direct roles in enzyme catalysis or binding of substrates, DNA or effectors, linking lysine chemistry and redox biology as a regulatory principle. NOS/SONOS switches are frequently found in proteins from human and plant pathogens, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and also in many human proteins with established roles in gene expression, redox signaling and homeostasis in physiological and pathophysiological conditions.

PubMed: 35165445
DOI: 10.1038/s41589-021-00966-5

実験手法

X-RAY DIFFRACTION (1.35 Å)