9R6U

Crystal structure of E. coli Adenylate kinase K47A mutant in complex with inhibitor Ap5A

9R6U の概要

• エントリーDOI: 10.2210/pdb9r6u/pdb
• 分子名称: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: adenylate kinase, k47a mutant, ap5a, protein dynamics, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49071.67

構造登録者

Phoeurk, C.,Wolf-Watz, M.,Sauer-Eriksson, A.E. (登録日: 2025-05-13, 公開日: 2025-10-15, 最終更新日: 2025-10-29)

主引用文献

Mattsson, J.,Phoeurk, C.,Schierholz, L.,Mushtaq, A.U.,Rodriguez Buitrago, J.A.,Rogne, P.,Sauer-Eriksson, A.E.,Wolf-Watz, M.
Exploring Helical Fraying Linked to Dynamics and Catalysis in Adenylate Kinase.
Biochemistry, 64:4281-4295, 2025

PubMed Abstract: Conformational dynamics is a fundamental aspect of enzymatic catalysis that, for example, can be linked to ligand binding and release, assembly of the active site, and the catalytic mechanism. The essential and metabolic enzyme adenylate kinase (AK) undergoes large-scale conformational changes in response to binding of its substrates ATP and AMP. As such, it has been intensely studied in search of linkages between dynamics and catalysis. For a complex conformational change to occur in a protein, whether it is of an induced fit or conformational selection nature, changes at several hinges are often required. Here, based on a comparative structure-function analysis of AK enzymes from and the archaea and from human AK1, we found that conformational changes in the enzymes are to a varying degree linked to bending, fraying, or unfolding/folding events of the termini of α-helices observed in various structural hot spots of the enzymes. The findings contribute with a mechanistic angle to how enzymatic dynamics and catalysis relate to the plasticity of the termini of α-helices.

PubMed: 41042980
DOI: 10.1021/acs.biochem.5c00306

実験手法

X-RAY DIFFRACTION (1.77 Å)