8CRG

E. coli adenylate kinase in complex with two ADP molecules as a result of enzymatic AP4A hydrolysis

8CRG の概要

• エントリーDOI: 10.2210/pdb8crg/pdb
• 分子名称: Adenylate kinase, ADENOSINE-5'-DIPHOSPHATE, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: phosphotransferase, energy metabolism, ap4a hydrolysis, potential moonlighting protein, transferase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49158.12

構造登録者

Oelker, M.,Tischlik, S.,Wolf-Watz, M.,Sauer-Eriksson, A.E. (登録日: 2023-03-08, 公開日: 2023-06-14, 最終更新日: 2023-10-25)

主引用文献

Tischlik, S.,Oelker, M.,Rogne, P.,Sauer-Eriksson, A.E.,Drescher, M.,Wolf-Watz, M.
Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase.
Biochemistry, 62:2238-2243, 2023

PubMed Abstract: Adenylate kinases play a crucial role in cellular energy homeostasis through the interconversion of ATP, AMP, and ADP in all living organisms. Here, we explore how adenylate kinase (AdK) from interacts with diadenosine tetraphosphate (AP4A), a putative alarmone associated with transcriptional regulation, stress, and DNA damage response. From a combination of EPR and NMR spectroscopy together with X-ray crystallography, we found that AdK interacts with AP4A with two distinct modes that occur on disparate time scales. First, AdK dynamically interconverts between open and closed states with equal weights in the presence of AP4A. On a much slower time scale, AdK hydrolyses AP4A, and we suggest that the dynamically accessed substrate-bound open AdK conformation enables this hydrolytic activity. The partitioning of the enzyme into open and closed states is discussed in relation to a recently proposed linkage between active site dynamics and collective conformational dynamics.

PubMed: 37418448
DOI: 10.1021/acs.biochem.3c00189

実験手法

X-RAY DIFFRACTION (1.49 Å)