Journal
BIOCHEMISTRY
Volume 50, Issue 48, Pages 10559-10565Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi201008f
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Funding
- National Science Foundation [MCB-0842743]
- University of Tennessee, Knoxville, TN
- U.S. Department of Energy EPSCoR [DE-FG02-08ER46528]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0842743] Funding Source: National Science Foundation
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NMR spectroscopy experiments and molecular dynamics simulations were performed to describe the dynamic properties of the aminoglycoside acetyltransferase (3)-IIIb (AAC) in its apo and coenzyme A (CoASH) bound forms. The N-15-H-1 HSQC spectra indicate a partial structural change and coupling of the CoASH binding site with another region in the protein upon the CoASH titration into the apo enzyme. Molecular dynamics simulations indicate a significant structural and dynamic variation of the long loop in the antibiotic binding domain in the form of a relatively slow (250 ns), concerted opening motion in the CoASH-enzyme complex and that binding of the CoASH increases the structural flexibility of the loop, leading to an interchange between several similar equally populated conformations.
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