4X8H: Crystal structure of E. coli Adenylate kinase P177A mutant

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.
PDB ID: 4X8HDownload
MMDB ID: 131119
PDB Deposition Date: 2014/12/10
Updated in MMDB: 2018/07
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4X8H: monomeric; determined by author and by software (PISA)
Molecular Components in 4X8H
Label Count Molecule
Protein (1 molecule)
Adenylate Kinase(Gene symbol: adk)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB