4X8O

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

Summary for 4X8O

• Entry DOI: 10.2210/pdb4x8o/pdb
• Related: 1ake
• Descriptor: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: adenylate kinase, y171w, ap5a, protein dynamics, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P69441
• Total number of polymer chains: 2
• Total formula weight: 49190.46

Authors

Sauer-Eriksson, A.E.,Kovermann, M.,Aden, J.,Grundstrom, C.,Wolf-Watz, M.,Sauer, U.H. (deposition date: 2014-12-10, release date: 2015-07-15, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)