Macromolecular Research, Vol.14, No.2, 166-172, April, 2006
The Allosteric Transition of the Chaperonin GroEL from Escherichia coli as Studied by Solution X-Ray Scattering
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This is a short review article of our recent studies on the ATP-induced, allosteric conformational transitionof the chaperonin GroEL complex by solution X-ray scattering. We used synchrotron X-ray scattering with a two-dimensional, charge-coupled, device-based X-ray detector to study (1) the specificity of the chaperonin GroEL forits ligand that induced the allosteric transition, and (2) the identification of the allosteric transition of GroEL in itscomplicated kinetics induced by ATP. Due to the dramatically increased sensitivity of the X-ray scattering techniquebased on the use of the two dimensional X-ray detector and synchrotron radiation, different allosteric conformationalstates of GroEL populated under different conditions were clearly distinguished from each other. It was concludedthat solution X-ray scattering is an extremely powerful tool for investigating the equilibrium and kinetics of coop-erative conformational transitions of oligomeric protein complex, especially when combined with other spectro-scopic techniques such as fluorescence spectroscopy.
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