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EF1 guanine nucleotide exchange domain

FieldValue
SymbolEF1_GNE
NameEF1_GNE
imagePDB 2b7c EBI.jpg
captionyeast guanine nucleotide exchange factor eef1balpha k205a mutant in complex with eef1a
PfamPF00736
InterProIPR014038
PROSITEPDOC00648
SCOP1b64
CDDcd00292

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).

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).

References

References

  1. (2001). "Structural studies of eukaryotic elongation factors". Cold Spring Harbor Symposia on Quantitative Biology.
  2. (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.
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