Send to

Choose Destination
Nat Commun. 2010 Nov 16;1:111.

Overlap between folding and functional energy landscapes for adenylate kinase conformational change.

Author information

Department of Chemistry, Chemical Biological Centre, Umeå University, Umeå 90187, Sweden.


Enzyme function is often dependent on fluctuations between inactive and active structural ensembles. Adenylate kinase isolated from Escherichia coli (AK(e)) is a small phosphotransfer enzyme in which interconversion between inactive (open) and active (closed) conformations is rate limiting for catalysis. AK(e) has a modular three-dimensional architecture with two flexible substrate-binding domains that interact with the substrates AMP, ADP and ATP. Here, we show by using a combination of biophysical and mutagenic approaches that the interconversion between open and closed states of the ATP-binding subdomain involves partial subdomain unfolding/refolding in an otherwise folded enzyme. These results provide a novel and, possibly general, molecular mechanism for the switch between open and closed conformations in AK(e).


LinkOut - more resources

Full Text Sources

Molecular Biology Databases

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center