EF1 guanine nucleotide exchange domain
From Wikipedia the free encyclopedia
| EF1_GNE | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 yeast guanine nucleotide exchange factor eef1balpha k205a mutant in complex with eef1a | |||||||||
| Identifiers | |||||||||
| Symbol | EF1_GNE | ||||||||
| Pfam | PF00736 | ||||||||
| InterPro | IPR014038 | ||||||||
| PROSITE | PDOC00648 | ||||||||
| SCOP2 | 1b64 / SCOPe / SUPFAM | ||||||||
| CDD | cd00292 | ||||||||
| |||||||||
In molecular biology, the EF1 guanine nucleotide exchange domain is a protein domain found in the beta and delta chains of elongation factors from eukaryotes and archaea.
Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta).[1]
The EF1 guanine nucleotide exchange domain is found in the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).[2]
References[edit]
- ^ Andersen GR, Nyborg J (2001). "Structural studies of eukaryotic elongation factors". Cold Spring Harbor Symposia on Quantitative Biology. 66: 425–37. doi:10.1101/sqb.2001.66.425. PMID 12762045.
- ^ Pérez JM, Siegal G, Kriek J, Hård K, Dijk J, Canters GW, Möller W (February 1999). "The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli". Structure. 7 (2): 217–26. doi:10.1016/S0969-2126(99)80027-6. PMID 10368288.