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The Mechanism for Activation of GTP Hydrolysis on the Ribosome
Open accessAbstract
A Likely Conformation: At several stages of protein synthesis, guanosine triphosphate hydrolyzing enzymes (GTPases) interact with the ribosome, and GTP hydrolysis is coupled to progression of synthesis. Voorhees et al. (p. 835 ) have determined a 3.2-resolution structure of the GTPase, elongation factor Tu, which delivers amino-acyl transfer RNA (tRNA) to the ribosome. The GTPase and tRNA were bound to the ribosome and were stalled in an active conformation by a GTP analog. The structure revealed that activation of the enzyme only required small changes in conformation to move a catalytic histidine into the correct position for hydrolysis. A similar mechanism likely applies to the activation of other translational GTPases.
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“In the GDPNP-bound form Tet(O) was earlier shown biochemically to promote release of Tc from the 70S ribosome 20,22, and the elucidation of the current structure therefore provides direct functional insights into the mechanisms of Tet(O)-mediated Tc resistance.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [20]
In the citing paper
“Moreover, binding of TetM to the ribosome induces A1492 and A1493 to adopt a flipped-out conformation (Fig. 2 C and D), analogous to that observed during decoding of the mRNA by EF-Tu•GTP•aa-tRNA (25) (Fig. 4D).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [25]
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“Finally, we observe that TetM also induces a conformation in the stalk base, analogous to that observed in the EF-Tu•70S structure (25).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [25]
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Metadata
- Authors
- Voorhees, R. M., Schmeing, T. M., Kelley, A. C., & Ramakrishnan, V.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Voorhees, Rebecca M.
- Schmeing, T. Martin
- Venue
- Science
- Published
- 2010-11-05
- Volume
- 330
- Issue
- 6005
- Pages
- 835-838
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3763471
- OpenAlex
- W2165048399
- Cited by
- 366
- References
- 34
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 6 · 2023: 10 · 2022: 23 · 2021: 13 · 2020: 20 · 2019: 16 · 2018: 23 · 2017: 17 · 2016: 31 · 2015: 30 · 2014: 31 · 2013: 46 · 2012: 39
- FWCI
- 16.30
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Wellcome Trust (082086)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- GTP hydrolysis, ribosome, elongation factor Tu, translational GTPases, aminoacyl-tRNA, catalytic histidine, sarcin-ricin loop, 23S rRNA, protein synthesis
- MeSH terms
- Bacterial Proteins, Enzyme Activation, Guanosine Triphosphate, Hydrolysis, Nucleic Acid Conformation, Paromomycin, Peptide Elongation Factor Tu, Phosphates, Ribosomes, RNA, Bacterial, RNA, Ribosomal, 23S, RNA, Transfer, Amino Acyl, Thermus thermophilus, Protein Structure, Tertiary, Crystallography, X-Ray, Catalytic Domain, Hydrophobic and Hydrophilic Interactions
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