Comment
doi: 10.1073/pnas.0812576106.
Epub 2009 Jan 21.
Visualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor Tu
Affiliations
- PMID: 19164543
- PMCID: PMC2633576
- DOI: 10.1073/pnas.0812576106
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Comment
Visualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor Tu
Proc Natl Acad Sci U S A.
.
No abstract available
Conflict of interest statement
The author declares no conflict of interest.
Figures
Mechanism of GTP hydrolysis in the α-subunit of heterotrimeric G proteins, in Ras-RasGAP, Sar-ArfGAP (modified from ref. 16), and the EF-Tu·aa-tRNA·ribosome complex. GTP-binding protein and the GTPase-activating protein (GAP) are shown in blue and red, respectively. GTP is shown in the transition state of hydrolysis; negative charges on phosphoryl groups are omitted for clarity.
Comment on
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Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1063-8. doi: 10.1073/pnas.0811370106. Epub 2009 Jan 2. Proc Natl Acad Sci U S A. 2009. PMID: 19122150 Free PMC article.
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- Kothe U, Rodnina MV. Delayed release of inorganic phosphate from elongation factor Tu following GTP hydrolysis on the ribosome. Biochemistry. 2006;45:12767–12774. - PubMed
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