GTP-binding elongation factor family, EF-Tu/EF-1A subfamily
| Elongation factor Tu GTP binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 eif2gamma apo | |||||||||
| Identifiers | |||||||||
| Symbol | GTP_EFTU | ||||||||
| Pfam | PF00009 | ||||||||
| Pfam clan | CL0023 | ||||||||
| InterPro | IPR000795 | ||||||||
| PROSITE | PDOC00273 | ||||||||
| SCOP | 1etu | ||||||||
| SUPERFAMILY | 1etu | ||||||||
| CDD | cd00881 | ||||||||
| |||||||||
| Elongation factor Tu domain 2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
eif2gamma apo | |||||||||
| Identifiers | |||||||||
| Symbol | GTP_EFTU_D2 | ||||||||
| Pfam | PF03144 | ||||||||
| InterPro | IPR004161 | ||||||||
| PROSITE | PDOC00273 | ||||||||
| SCOP | 1etu | ||||||||
| SUPERFAMILY | 1etu | ||||||||
| CDD | cd01342 | ||||||||
| |||||||||
| Elongation factor Tu C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 whole, unmodified, ef-tu(elongation factor tu). | |||||||||
| Identifiers | |||||||||
| Symbol | GTP_EFTU_D3 | ||||||||
| Pfam | PF03143 | ||||||||
| InterPro | IPR004160 | ||||||||
| SCOP | 1etu | ||||||||
| SUPERFAMILY | 1etu | ||||||||
| CDD | cd01513 | ||||||||
| |||||||||
In molecular biology, the GTP-binding elongation factor family, EF-Tu/EF-1A subfamily is a family of elongation factors, which includes the eukaryotic eEF-1 and the prokaryotic EF-Tu.
These proteins consist of three structural domains: the GTP-binding domain, and two oligonucleotide binding domains that are often referred to as domain 2 and domain 3.
The GTP-binding domain has been shown [1] to be involved in a conformational change mediated by the hydrolysis of GTP to GDP. This region is conserved in both EF-1alpha/EF-Tu and also in EF-2/EF-G and thus seems typical for GTP-dependent proteins which bind non-initiator tRNAs to the ribosome. The GTP-binding protein synthesis factor family also includes the eukaryotic peptide chain release factor GTP-binding subunits [2] and prokaryotic peptide chain release factor 3 (RF-3);[3] the prokaryotic GTP-binding protein lepA and its homologue in yeast (GUF1) and Caenorhabditis elegans (ZK1236.1); yeast HBS1;[4] rat statin S1;[5] and the prokaryotic selenocysteine-specific elongation factor selB.[6]
Domain 2 adopts a beta-barrel structure, and is involved in binding to charged tRNA.[7] This domain is structurally related to the C-terminal domain of EF2, to which it displays weak sequence similarity. This domain is also found in other proteins such as translation initiation factor IF-2 and tetracycline-resistance proteins.
Domain 3 represents the C-terminal domain, which adopts a beta-barrel structure, and is involved in binding to both charged tRNA and to EF1B (or EF-Ts).[8]
References
- ↑ Moller W, Schipper A, Amons R (September 1987). "A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs". Biochimie 69 (9): 983–9. doi:10.1016/0300-9084(87)90232-X. PMID 3126836.
- ↑ Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF (September 1995). "The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae". EMBO J. 14 (17): 4365–73. PMC 394521. PMID 7556078.
- ↑ Grentzmann G, Brechemier-Baey D, Heurgué-Hamard V, Buckingham RH (May 1995). "Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals". J. Biol. Chem. 270 (18): 10595–600. doi:10.1074/jbc.270.18.10595. PMID 7737996.
- ↑ Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA (October 1992). "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis". Cell 71 (1): 97–105. doi:10.1016/0092-8674(92)90269-I. PMID 1394434.
- ↑ Ann DK, Moutsatsos IK, Nakamura T, Lin HH, Mao PL, Lee MJ, Chin S, Liem RK, Wang E (June 1991). "Isolation and characterization of the rat chromosomal gene for a polypeptide (pS1) antigenically related to statin". J. Biol. Chem. 266 (16): 10429–37. PMID 1709933.
- ↑ Forchhammer K, Leinfelder W, Bock A (November 1989). "Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein". Nature 342 (6248): 453–6. doi:10.1038/342453a0. PMID 2531290.
- ↑ Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J (December 1995). "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog". Science 270 (5241): 1464–72. doi:10.1126/science.270.5241.1464. PMID 7491491.
- ↑ Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB (August 1997). "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus". Nat. Struct. Biol. 4 (8): 650–6. doi:10.1038/nsb0897-650. PMID 9253415.
This article incorporates text from the public domain Pfam and InterPro IPR000795
This article incorporates text from the public domain Pfam and InterPro IPR004161
This article incorporates text from the public domain Pfam and InterPro IPR004160