4X8O

Crystal structure of E. coli Adenylate kinase Y171W mutant in complex with inhibitor Ap5a

4X8O の概要

• エントリーDOI: 10.2210/pdb4x8o/pdb
• 関連するPDBエントリー: 1ake
• 分子名称: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: adenylate kinase, y171w, ap5a, protein dynamics, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P69441
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49190.46

構造登録者

Sauer-Eriksson, A.E.,Kovermann, M.,Aden, J.,Grundstrom, C.,Wolf-Watz, M.,Sauer, U.H. (登録日: 2014-12-10, 公開日: 2015-07-15, 最終更新日: 2024-01-10)

主引用文献

Kovermann, M.,Aden, J.,Grundstrom, C.,Elisabeth Sauer-Eriksson, A.,Sauer, U.H.,Wolf-Watz, M.
Structural basis for catalytically restrictive dynamics of a high-energy enzyme state.
Nat Commun, 6:7644-7644, 2015

PubMed Abstract: An emerging paradigm in enzymology is that transient high-energy structural states play crucial roles in enzymatic reaction cycles. Generally, these high-energy or 'invisible' states cannot be studied directly at atomic resolution using existing structural and spectroscopic techniques owing to their low populations or short residence times. Here we report the direct NMR-based detection of the molecular topology and conformational dynamics of a catalytically indispensable high-energy state of an adenylate kinase variant. On the basis of matching energy barriers for conformational dynamics and catalytic turnover, it was found that the enzyme's catalytic activity is governed by its dynamic interconversion between the high-energy state and a ground state structure that was determined by X-ray crystallography. Our results show that it is possible to rationally tune enzymes' conformational dynamics and hence their catalytic power--a key aspect in rational design of enzymes catalysing novel reactions.

PubMed: 26138143
DOI: 10.1038/ncomms8644

実験手法

X-RAY DIFFRACTION (2.1 Å)