Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex
- PMID: 11373622
- DOI: 10.1038/88598
Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex
Abstract
In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1Balpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Balpha are consistent with in vivo data. The base, sugar and alpha-phosphate bind as in other known nucleotide G-protein complexes, whereas the beta- and gamma-phosphates are disordered. A mutation of Lys 205 in eEF1Balpha that inserts into the Mg2+ binding site of eEF1A is lethal. This together with the structures emphasizes the essential role of Mg2+ in nucleotide exchange in the eEF1A-eEF1Balpha complex.
Similar articles
-
Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.Mol Cell. 2000 Nov;6(5):1261-6. doi: 10.1016/s1097-2765(00)00122-2. Mol Cell. 2000. PMID: 11106763
-
Structural basis for the binding of didemnins to human elongation factor eEF1A and rationale for the potent antitumor activity of these marine natural products.J Med Chem. 2004 Aug 26;47(18):4439-52. doi: 10.1021/jm0306428. J Med Chem. 2004. PMID: 15317456
-
Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.Nucleic Acids Res. 2014 Nov 10;42(20):12939-48. doi: 10.1093/nar/gku974. Epub 2014 Oct 17. Nucleic Acids Res. 2014. PMID: 25326326 Free PMC article.
-
[Functional compartmentation of the translation apparatus and channeling of tRNA/aminoacyl-tRNA in cells of higher eukaryotes].Mol Biol (Mosk). 2001 Jul-Aug;35(4):702-7. Mol Biol (Mosk). 2001. PMID: 11524957 Review. Russian.
-
The role of translation elongation factor eEF1 subunits in neurodevelopmental disorders.Hum Mutat. 2019 Feb;40(2):131-141. doi: 10.1002/humu.23677. Epub 2018 Nov 23. Hum Mutat. 2019. PMID: 30370994 Review.
Cited by
-
Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B.J Biol Chem. 2015 Apr 3;290(14):8694-710. doi: 10.1074/jbc.M114.628594. Epub 2015 Jan 29. J Biol Chem. 2015. PMID: 25635048 Free PMC article.
-
Rapid evolution in conformational space: a study of loop regions in a ubiquitous GTP binding domain.Protein Sci. 2004 Mar;13(3):608-16. doi: 10.1110/ps.03299804. Protein Sci. 2004. PMID: 14978301 Free PMC article.
-
Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria.Nucleic Acids Res. 2003 Jul 15;31(14):4227-37. doi: 10.1093/nar/gkg440. Nucleic Acids Res. 2003. PMID: 12853641 Free PMC article.
-
GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5·Vps9 system.J Biol Chem. 2010 Nov 19;285(47):36689-97. doi: 10.1074/jbc.M110.152132. Epub 2010 Sep 10. J Biol Chem. 2010. PMID: 20833725 Free PMC article.
-
Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis.Plant Physiol. 2011 Apr;155(4):1769-78. doi: 10.1104/pp.110.165852. Epub 2011 Feb 10. Plant Physiol. 2011. PMID: 21311030 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
Grants and funding
LinkOut - more resources
Other Literature Sources
Molecular Biology Databases
Miscellaneous