Recombinant Escherichia coli Adenylate kinase (adk)

1. These results are consistent with an induced-fit model in which the transition of AdK from an open state to a closed state is initiated by ATP binding. PMID: 28767234
2. Fast closure of N-terminal long loops but slow formation of beta strands precedes the folding transition state of Escherichia coli adenylate kinase. PMID: 24787383
3. As both open and closed states sampled a wide range of conformation transitions, our simulation strongly supported the conformational selection mechanism for Escherichia coli ADK. PMID: 23936827
4. fast subdomain folding prior to global refolding transition of adenylate kinase; applied double kinetics method to test the hypothesis that specific short native-like intramolecular distances between residues separated by long chain segments in a globular protein can be formed in the collapsed state, prior to the cooperative folding transition PMID: 22898349
5. In Cartesian space, LID domain closure precedes NMP domain closure in the bound simulation, consistent with prior coarse-grained models of the adenylate kinase conformational transition. PMID: 20471396
6. Results demonstrate that the conformational ensemble of adenylate kinase is significantly populated by a locally unfolded state and that the excited-state can be manipulated through mutation, independent of perturbations of the ground-state structures. PMID: 19805185
7. The dynamics of adenylate kinase of Escherichia coli, and its complex with the inhibitor AP(5)A, are characterized PMID: 15382240
8. Simulation supports the hypothesis that hydrogen bonds between AMP's adenine and the protein are at the origin of the high nucleoside monophosphate (NMP) specificity of adenylate kinase PMID: 15521058
9. AK molecules undergo fast collapse to an ensemble of compact structures where the local environment of surface probes seems to be native-like but the two labeled secondary structure elements remain unfolded. PMID: 16098987
10. Data describe the plastic network model, used to generate a conformational change pathway for Escherichia coli adenylate kinase based on two crystal structures, namely that of an open and a closed conformer. PMID: 16139299
11. Adenylate kinase from E coli have two highly flexible domains which close over bound substrates. PMID: 16302237
12. for adenylate kinase, the change in the number of interdomain contacting atoms upon closure showed a considerable increase, suggesting that adk undergoes closure through a hinge mechanism PMID: 17299745
13. Results describe the atomistic mechanism of conformational transition in adenylate kinase. PMID: 18682219
14. Results show that the flexible subdomains of adk fold into their native structure in a noncooperative manner with respect to the CORE subdomain. PMID: 19219996

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KEGG: ecj:JW0463

STRING: 316385.ECDH10B_0430