The Ribosomal Peptidyl Transferase
نویسندگان
چکیده
منابع مشابه
The ribosomal peptidyl transferase.
Peptide bond formation on the ribosome takes place in an active site composed of RNA. Recent progress of structural, biochemical, and computational approaches has provided a fairly detailed picture of the catalytic mechanism of the reaction. The ribosome accelerates peptide bond formation by lowering the activation entropy of the reaction due to positioning the two substrates, ordering water in...
متن کاملThe ribosomal peptidyl transferase center: structure, function, evolution, inhibition.
The ribosomal peptidyl transferase center (PTC) resides in the large ribosomal subunit and catalyzes the two principal chemical reactions of protein synthesis: peptide bond formation and peptide release. The catalytic mechanisms employed and their inhibition by antibiotics have been in the focus of molecular and structural biologists for decades. With the elucidation of atomic structures of the...
متن کاملInteraction of pleuromutilin derivatives with the ribosomal peptidyl transferase center.
Tiamulin is a pleuromutilin antibiotic that is used in veterinary medicine. The recently published crystal structure of a tiamulin-50S ribosomal subunit complex provides detailed information about how this drug targets the peptidyl transferase center of the ribosome. To promote rational design of pleuromutilin-based drugs, the binding of the antibiotic pleuromutilin and three semisynthetic deri...
متن کاملIdentification of a ribosomal protein essential for peptidyl transferase activity.
Extraction with 2 M lithium chloride removes a group of proteins (LiC1 SP) from 50S ribosomal subunits. Both the LiC1 SP and the resulting cores, which contain the remaining proteins as well as 5S and 23S RNA, lack peptidyl transferase activity, as measured by the "fragment reaction". Activity can be restored to the LiC1 cores by reconstitution with LiC1 SP under conditions of high temperature ...
متن کاملThe oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning.
The oxazolidinones represent the first new class of antibiotics to enter into clinical usage within the past 30 years, but their binding site and mechanism of action has not been fully characterized. We have determined the crystal structure of the oxazolidinone linezolid bound to the Deinococcus radiodurans 50S ribosomal subunit. Linezolid binds in the A site pocket at the peptidyltransferase c...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2007
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2007.03.015