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

Ulrika Olsson and Magnus Wolf-Watz ()
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Ulrika Olsson: Chemical Biological Centre, Umeå University
Magnus Wolf-Watz: Chemical Biological Centre, Umeå University

Nature Communications, 2010, vol. 1, issue 1, 1-8

Abstract: Abstract Enzyme function is often dependent on fluctuations between inactive and active structural ensembles. Adenylate kinase isolated from Escherichia coli (AKe) is a small phosphotransfer enzyme in which interconversion between inactive (open) and active (closed) conformations is rate limiting for catalysis. AKe 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 AKe.

Date: 2010
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DOI: 10.1038/ncomms1106

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