J
Jack A. Dunkle
Researcher at University of Alabama
Publications - 28
Citations - 1782
Jack A. Dunkle is an academic researcher from University of Alabama. The author has contributed to research in topics: Translation (biology) & Ribosomal RNA. The author has an hindex of 15, co-authored 22 publications receiving 1581 citations. Previous affiliations of Jack A. Dunkle include Emory University & University of California, Berkeley.
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Journal ArticleDOI
Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action.
TL;DR: X-ray crystal structures of the Escherichia coli ribosome in complexes with clinically important antibiotics of four major classes are reported, arguing that the identity of nucleotides 752, 2609, and 2055 of 23S ribosomal RNA explain in part the spectrum and selectivity of antibiotic action.
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Structures of the Bacterial Ribosome in Classical and Hybrid States of tRNA Binding
Jack A. Dunkle,Leyi Wang,Michael Feldman,Michael Feldman,Arto Pulk,Vincent B. Chen,Gary J. Kapral,Jonas Noeske,Jane S. Richardson,Scott C. Blanchard,Jamie H. D. Cate,Jamie H. D. Cate +11 more
TL;DR: Two crystal structures indicate how conformational changes in the ribosome assist protein synthesis and help to explain how the ratchet-like motion of the two ribosomal subunits contributes to the mechanisms of translocation, termination, and Ribosome recycling.
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Structures of the ribosome in intermediate states of ratcheting.
TL;DR: In this article, the authors describe x-ray crystal structures of the intact Escherichia coli ribosome, either in the apo-form (3.5 angstrom resolution) or with one (4.0 angstrom-resolution) or two(4.1-resolution)-antimodal stem-loop tRNA mimics bound, that reveal intermediate states of intersubunit rotation.
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The Mechanisms of RNA SHAPE Chemistry
TL;DR: Analysis of SHAPE conformations revealed that 2'-hydroxyl reactivity is broadly facilitated by general base catalysis involving multiple RNA functional groups and by two specific orientations of the bridging 3'-phosphate group.
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Binding and Action of CEM-101, a New Fluoroketolide Antibiotic That Inhibits Protein Synthesis
Beatriz Llano-Sotelo,Jack A. Dunkle,Dorota Klepacki,Wen Zhang,Prabhavathi Fernandes,Jamie H. D. Cate,Jamie H. D. Cate,Alexander S. Mankin +7 more
TL;DR: The results of chemical probing suggest that the orientation of the C EM-101 extended side chain observed in the E. coli ribosome closely resembles its placement in Staphylococcus aureus ribosomes and thus likely accurately reflects interaction of CEM-101 with the ribosites of the pathogenic bacterial targets of the drug.