Peptidyl transferase: ancient and exiguous
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 کاملPeptidyl Transferase Center and the Emergence of the Translation System
In this work, the three-dimensional (3D) structure of the ancestral Peptidyl Transferase Center (PTC) built by concatamers of ancestral sequences of tRNAs was reconstructed, and its possible interactions with tRNAs molecules were analyzed. The 3D structure of the ancestral PTC was also compared with the current PTC of T. thermophilus. Docking experiments between the ancestral PTC and tRNAs sugg...
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 کاملPeptidyl transferase activity of tRNA: a quantum chemical study.
The mechanism of protein synthesis is still unknown due to inability to detect the so-called enzyme "peptidyl transferase" even after elucidation of high-resolution crystal structure of ribosome. We have recently shown by model building and semi-empirical energy calculation that the tRNA molecule at P-site of ribosome may act as peptidyl transferase (Das et al. (1999) J. Theor. Biol. 200, 193-2...
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 ...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2000
ISSN: 1074-5521
DOI: 10.1016/s1074-5521(00)00027-2