6S36

Crystal structure of E. coli Adenylate kinase R119K mutant

6S36 の概要

• エントリーDOI: 10.2210/pdb6s36/pdb
• 分子名称: Adenylate kinase, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: adenylate kinase, r119k variant, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23769.98

構造登録者

Grundstrom, C.,Rogne, P.,Wolf-Watz, M.,Sauer-Eriksson, A.E. (登録日: 2019-06-24, 公開日: 2019-08-07, 最終更新日: 2024-01-24)

主引用文献

Rogne, P.,Andersson, D.,Grundstrom, C.,Sauer-Eriksson, E.,Linusson, A.,Wolf-Watz, M.
Nucleation of an Activating Conformational Change by a Cation-pi Interaction.
Biochemistry, 58:3408-3412, 2019

PubMed Abstract: As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-π interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-π interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design.

PubMed: 31339702
DOI: 10.1021/acs.biochem.9b00538

実験手法

X-RAY DIFFRACTION (1.6 Å)