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

Author

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  • Ulrika Olsson

    (Chemical Biological Centre, Umeå University)

  • Magnus Wolf-Watz

    (Chemical Biological Centre, Umeå University)

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.

Suggested Citation

  • Ulrika Olsson & Magnus Wolf-Watz, 2010. "Overlap between folding and functional energy landscapes for adenylate kinase conformational change," Nature Communications, Nature, vol. 1(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1106
    DOI: 10.1038/ncomms1106
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    Cited by:

    1. Santiago Esteban-Martín & Robert Bryn Fenwick & Jörgen Ådén & Benjamin Cossins & Carlos W Bertoncini & Victor Guallar & Magnus Wolf-Watz & Xavier Salvatella, 2014. "Correlated Inter-Domain Motions in Adenylate Kinase," PLOS Computational Biology, Public Library of Science, vol. 10(7), pages 1-7, July.

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