Science (American Association for the Advancement of Science), 2010-11, Vol.330 (6005), p.835-838
2010
Details
- Autor(en) / Beteiligte
- Titel
- Mechanism for Activation of GTP Hydrolysis on the Ribosome
- Ist Teil von
- Science (American Association for the Advancement of Science), 2010-11, Vol.330 (6005), p.835-838
- Ort / Verlag
- Washington, DC: American Association for the Advancement of Science
- Erscheinungsjahr
- 2010
- Link zum Volltext
- Quelle
- American Association for the Advancement of Science
- Beschreibungen/Notizen
- Protein synthesis requires several guanosine triphosphatase (GTPase) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-transfer RNAs (tRNAs) to the ribosome. To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. EF-Tu is in its active conformation, the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the γ-phosphate of GTP. This activated conformation is due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. The structure suggests a universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.1194460Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3763471
- Format
- –
- Schlagworte
- Active sites, Bacterial Proteins - chemistry, Bacterial Proteins - metabolism, Biochemistry, Biological and medical sciences, Catalysis, Catalytic Domain, Codons, Crystalline structure, Crystallography, X-Ray, Enzyme Activation, Enzyme kinetics, Fundamental and applied biological sciences. Psychology, Guanosine Triphosphate - analogs & derivatives, Guanosine Triphosphate - metabolism, Hydrolysis, Hydrophobic and Hydrophilic Interactions, Molecular biophysics, Molecules, Nucleic Acid Conformation, Paromomycin - metabolism, Peptide Elongation Factor Tu - chemistry, Peptide Elongation Factor Tu - metabolism, Peptide elongation factors, Phosphates, Phosphates - metabolism, Protein Structure, Tertiary, Protein synthesis, Ribonucleic acid, Ribosomes, Ribosomes - metabolism, RNA, RNA, Bacterial - chemistry, RNA, Bacterial - metabolism, RNA, Ribosomal, 23S - chemistry, RNA, Ribosomal, 23S - metabolism, RNA, Transfer, Amino Acyl - chemistry, RNA, Transfer, Amino Acyl - metabolism, Structure in molecular biology, Thermus thermophilus - chemistry, Thermus thermophilus - metabolism, Thermus thermophilus - ultrastructure, Transfer RNA