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Medicinal-Pharmaceutical Chemistry Commons

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Selected Works

Erika A. Taylor, Ph.D.

Chemicals and Drugs

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Full-Text Articles in Medicinal-Pharmaceutical Chemistry

Methyl Transfer By Substrate Signaling From A Knotted Protein Fold, Thomas Christian, Reiko Sakaguchi, Agata P. Perlinska, George Lahoud, Takuhiro Ito, Erika A. Taylor, Shigeyuki Yokoyama, Joanna I. Sulkowska, Ya-Ming Hou Dec 2015

Methyl Transfer By Substrate Signaling From A Knotted Protein Fold, Thomas Christian, Reiko Sakaguchi, Agata P. Perlinska, George Lahoud, Takuhiro Ito, Erika A. Taylor, Shigeyuki Yokoyama, Joanna I. Sulkowska, Ya-Ming Hou

Erika A. Taylor, Ph.D.

Proteins with knotted configurations, in comparison with unknotted proteins, are restricted in conformational space. Little is known regarding whether knotted proteins have sufficient dynamics to communicate between spatially separated substrate-binding sites. TrmD is a bacterial methyltransferase that uses a knotted protein fold to catalyze methyl transfer from S-adenosyl methionine (AdoMet) to G37-tRNA. The product, m1G37-tRNA, is essential for life and maintains protein-synthesis reading frames. Using an integrated approach of structural, kinetic, and computational analysis, we show that the structurally constrained TrmD knot is required for its catalytic activity. Unexpectedly, the TrmD knot undergoes complex internal movements that respond to AdoMet ...