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FEBS Lett. 2011 Jul 21;585(14):2158-64. doi: 10.1016/j.febslet.2011.05.041. Epub 2011 May 27.

Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization.

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  • 1Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago, Chile.


Phosphofructokinase-2 is a 66 kD homodimer whose subunits are associated by means of a bimolecular domain, the β-clasp, which is linked to the larger portion of each subunit by a reentrant chain topology. To investigate how this structural organization determines the folding pathway of Pfk-2, unfolding and folding kinetic experiments were performed. The folding pathway shows an unstructured monomeric intermediate and that most part of the dimer structure is reached as a slow concerted folding/association step with a quite folded transition state in terms of solvent exposure. Unfolding kinetics show a transient intermediate, probably a partially unfolded dimer. We propose that these characteristics arise by a mutual constrain between the large domain and the β-clasp domain imposed by their interrupted chain connectivity.

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