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  • BibTeX
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Science (American Association for the Advancement of Science), 2000-08, Vol.289 (5481), p.920-930
2000

Details

Autor(en) / Beteiligte
Titel
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Ist Teil von
  • Science (American Association for the Advancement of Science), 2000-08, Vol.289 (5481), p.920-930
Ort / Verlag
Washington, DC: American Society for the Advancement of Science
Erscheinungsjahr
2000
Link zum Volltext
Quelle
American Association for the Advancement of Science
Beschreibungen/Notizen
  • Using the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with two substrate analogs, we establish that the ribosome is a ribozyme and address the catalytic properties of its all-RNA active site. Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side-chain atoms closer than about 18 angstroms to the peptide bond being synthesized. The mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases, with the base of A2486 (A2451 in Escherichia coli) playing the same general base role as histidine-57 in chymotrypsin. The unusual pKa(where Kais the acid dissociation constant) required for A2486 to perform this function may derive in part from its hydrogen bonding to G2482 (G2447 in E. coli), which also interacts with a buried phosphate that could stabilize unusual tautomers of these two bases. The polypeptide exit tunnel is largely formed by RNA but has significant contributions from proteins L4, L22, and L39e, and its exit is encircled by proteins L19, L22, L23, L24, L29, and L31e.
Sprache
Englisch
Identifikatoren
ISSN: 0036-8075
eISSN: 1095-9203
DOI: 10.1126/science.289.5481.920
Titel-ID: cdi_proquest_miscellaneous_743521665
Format
–
Schlagworte
Active sites, Analytical, structural and metabolic biochemistry, Archaeal Proteins - chemistry, Archaeal Proteins - metabolism, Atoms, Bacteria, Base Pairing, Base Sequence, Binding Sites, Biochemistry, Biological and medical sciences, Catalysis, Chemical bases, Chemistry, Crystallization, Escherichia coli, Evolution, Molecular, Fundamental and applied biological sciences. Psychology, Haloarcula marismortui, Haloarcula marismortui - chemistry, Haloarcula marismortui - metabolism, Haloarcula marismortui - ultrastructure, Hydrogen Bonding, Hydrogen bonds, Hydrogen-Ion Concentration, L22 protein, L39e protein, L4 protein, Models, Molecular, Molecular Sequence Data, Molecular structure, Molecules, Nucleic Acid Conformation, Nucleic acids, Oligonucleotides - metabolism, Peptide Biosynthesis, Peptide synthesis, Peptides, Peptides - metabolism, Peptidyl Transferases - antagonists & inhibitors, Peptidyl Transferases - chemistry, Peptidyl Transferases - metabolism, Phosphates, Phosphates - chemistry, Phosphates - metabolism, Protein Conformation, Protein synthesis, Proteins, Puromycin - metabolism, Ribonucleic acid, Ribosomal Proteins - chemistry, Ribosomal Proteins - metabolism, Ribosomes, Ribosomes - chemistry, Ribosomes - metabolism, RNA, RNA, Archaeal - chemistry, RNA, Archaeal - metabolism, RNA, Catalytic - chemistry, RNA, Catalytic - metabolism, Rna, ribonucleoproteins, RNA, Ribosomal, 23S - chemistry, RNA, Ribosomal, 23S - metabolism, RNA, Transfer - metabolism, RNA, Transfer, Amino Acyl - metabolism, Space life sciences, Structure, Synthesis, Transfer RNA, Tunnels

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