Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.

Abstract:

:Escherichia coli phosphofructokinase-2 (Pfk-2) is a homodimer whose subunits consist of a large domain and an additional beta-sheet that provides the interfacial contacts between the subunits, creating a beta-barrel flattened-like structure with the adjacent subunit's beta-sheet. To determine how the structural organization of Pfk-2 determines its stability, the reversible unfolding of the enzyme was characterized under equilibrium conditions by enzymatic activity, circular dichroism, fluorescence and hydrodynamic measurements. Pfk-2 undergoes a cooperative unfolding/dissociation process with the accumulation of an expanded and unstructured monomeric intermediate with a marginal stability and a large solvent accessibility with respect to the native dimer.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Baez M,Babul J

doi

10.1016/j.febslet.2009.05.034

subject

Has Abstract

pub_date

2009-06-18 00:00:00

pages

2054-60

issue

12

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00405-0

journal_volume

583

pub_type

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