Comprehensive characterization of ligand‐induced plasticity changes in a dimeric enzyme

An enzyme's inherent structural plasticity is frequently associated with substrate binding, yet detailed structural characterization of flexible proteins remains challenging. This study employs complementary biophysical methods to characterize the partially unfolded structure of substrate‐free...

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Veröffentlicht in:	The FEBS journal 2016-08, Vol.283 (16), p.3029-3038
Hauptverfasser:	Baettig, Oliver M., Shi, Kun, Yachnin, Brahm J., Burk, David L., Berghuis, Albert M.
Format:	Artikel
Sprache:	eng
Schlagworte:	acetyl coenzyme A Acetyl Coenzyme A - chemistry Acetyltransferases - chemistry allosteric cooperativity aminoglycoside 6′‐N‐acetyltransferase type‐Ii aminoglycosides antibiotic resistance Bacterial Proteins - chemistry Circular Dichroism circular dichroism spectroscopy Crystal structure Crystallography, X-Ray dimerization Enterococcus faecium Enterococcus faecium - enzymology Enzymes Ligands ligand‐induced plasticity Models, Molecular Molecular biology Original Protein Conformation protein flexibility Protein Multimerization proteins Scattering, Small Angle X-radiation X-Ray Diffraction
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