Abstract
A combination of (15)N[(19)F], (31)P[(15)N], and (31)P[(19)F] rotational-echo double-resonance NMR has been used to characterize the conformation of a bound trifluoromethylketal, shikimate-based bisubstrate inhibitor of 5-enolpyruvylshikimate-3-phosphate synthase. The solid-state NMR experiments were performed on the complex formed in solution and then lyophilized at low temperatures in the presence of stabilizing lyoprotectants. The results of these experiments indicate that none of the side chains of the six arginines that surround the active site forms a compact salt bridge with the phosphate groups of the bound inhibitor.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3-Phosphoshikimate 1-Carboxyvinyltransferase
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Alkyl and Aryl Transferases / antagonists & inhibitors
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Alkyl and Aryl Transferases / chemistry*
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Alkyl and Aryl Transferases / metabolism*
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Arginine / chemistry
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / metabolism*
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Magnetic Resonance Spectroscopy / methods*
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Models, Molecular
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Molecular Conformation
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Phosphorus Isotopes
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Protein Conformation
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Shikimic Acid / analogs & derivatives*
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Shikimic Acid / chemistry
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Shikimic Acid / metabolism
Substances
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Enzyme Inhibitors
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Phosphorus Isotopes
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5-enolpyruvoylshikimate-3-phosphate
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Shikimic Acid
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Arginine
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Alkyl and Aryl Transferases
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3-Phosphoshikimate 1-Carboxyvinyltransferase