Results 11 to 20 of about 33,890 (233)

Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin [PDF]

open access: goldBMC Biology, 2004
Background The bacterial ribosome is a primary target of several classes of antibiotics. Investigation of the structure of the ribosomal subunits in complex with different antibiotics can reveal the mode of inhibition of ribosomal protein synthesis ...
Fucini Paola   +4 more
doaj   +2 more sources

The Peptidyl Transferase Center: a Window to the Past. [PDF]

open access: yesMicrobiol Mol Biol Rev, 2021
In his 2001 article, “Translation: in retrospect and prospect,” the late Carl Woese made a prescient observation that there was a need for the then-current view of translation to be “reformulated to become an all-embracing perspective about which 21st century Biology can develop” (RNA 7:1055–1067, 2001, https://doi.org/10.1017 ...
Tirumalai MR, Rivas M, Tran Q, Fox GE.
europepmc   +3 more sources

Substrate Specificity of Escherichia coli Peptidyl‐Transferase [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1970
The kinetics of the puromycin interaction with different ribosomal bound peptidyl‐tRNAs were studied. The rates of the puromycin reaction with AA‐Phe‐tRNA and AA2‐Phe‐tRNA using three different amino acids (AA) were compared. At 4° all the three dipeptidyl‐tRNAsPhe reacted considerably slower than the three tripeptidyl‐tRNAsPhe. Acetyl‐Phe‐tRNA reacted
Amos Panet, Nathan de Groot, Y. Lapidot
openalex   +4 more sources

Hydrolysis of fMet-tRNA by Peptidyl Transferase [PDF]

open access: greenProceedings of the National Academy of Sciences, 1971
Escherichia coli and rabbit reticulocyte (f[ 3 H]Met-tRNA·AUG·ribosome) intermediates undergo hydrolysis, with release of f[ 3 H]methionine, upon addition of tRNA or CpCpA in the presence of acetone.
C. Thomas Caskey   +3 more
openalex   +4 more sources

Structural insights into context-specific inhibition of bacterial translation by macrolides [PDF]

open access: yesNature Communications
The ribosome’s peptidyl transferase center (PTC) catalyzes peptide bond formation during protein synthesis and is targeted by many antibiotic classes. Remarkably, macrolides that bind in the peptide exit tunnel some ~10 Å away from the PTC also remotely ...
Egor A. Syroegin   +5 more
doaj   +2 more sources

Peptidyl transferase center activity observed in single ribosomes

open access: hybridJournal of Molecular Biology, 1999
We demonstrate the functional activity of single ribosomal complexes, opening the way for detailed studies of the trajectories of protein synthesis. Our approach employs a single-molecule detection system, capable of picoseconds to minutes resolution, to observe a growing peptide labeled at its N terminus with the fluorophore tetramethylrhodamine (TMR).
Alexander Sytnik   +5 more
openalex   +3 more sources

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. [PDF]

open access: yesNat Struct Mol Biol, 2009
Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs.
Voorhees RM   +4 more
europepmc   +4 more sources

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