5G3Z

Crystal structure of adenylate kinase ancestor 3 with Zn, Mg and Ap5A bound

5G3Z の概要

• エントリーDOI: 10.2210/pdb5g3z/pdb
• 関連するPDBエントリー: 5G3Y 5G40 5G41
• 分子名称: ADENYLATE KINSE, ZINC ION, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: adenylate kinase, adp, transferase, phosphoryl transfer, nucleotide-binding
• 由来する生物種: SYNTHETIC CONSTRUCT
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25175.92

構造登録者

Nguyen, V.,Kutter, S.,English, J.,Kern, D. (登録日: 2016-05-03, 公開日: 2016-12-28, 最終更新日: 2024-01-10)

主引用文献

Nguyen, V.,Wilson, C.,Hoemberger, M.,Stiller, J.B.,Agafonov, R.V.,Kutter, S.,English, J.,Theobald, D.L.,Kern, D.
Evolutionary drivers of thermoadaptation in enzyme catalysis.
Science, 355:289-294, 2017

PubMed Abstract: With early life likely to have existed in a hot environment, enzymes had to cope with an inherent drop in catalytic speed caused by lowered temperature. Here we characterize the molecular mechanisms underlying thermoadaptation of enzyme catalysis in adenylate kinase using ancestral sequence reconstruction spanning 3 billion years of evolution. We show that evolution solved the enzyme's key kinetic obstacle-how to maintain catalytic speed on a cooler Earth-by exploiting transition-state heat capacity. Tracing the evolution of enzyme activity and stability from the hot-start toward modern hyperthermophilic, mesophilic, and psychrophilic organisms illustrates active pressure versus passive drift in evolution on a molecular level, refutes the debated activity/stability trade-off, and suggests that the catalytic speed of adenylate kinase is an evolutionary driver for organismal fitness.

PubMed: 28008087
DOI: 10.1126/science.aah3717

実験手法

X-RAY DIFFRACTION (1.89 Å)