 |
PDBsum entry 3e20
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
261 a.a.
|
|
|
|
|
|
|
|
|
|
|
175 a.a.
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural insights into erf3 and stop codon recognition by erf1.
|
|
|
Authors
|
|
Z.Cheng,
K.Saito,
A.V.Pisarev,
M.Wada,
V.P.Pisareva,
T.V.Pestova,
M.Gajda,
A.Round,
C.Kong,
M.Lim,
Y.Nakamura,
D.I.Svergun,
K.Ito,
H.Song.
|
|
|
Ref.
|
|
Genes Dev, 2009,
23,
1106-1118.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Eukaryotic translation termination is mediated by two interacting release
factors, eRF1 and eRF3, which act cooperatively to ensure efficient stop codon
recognition and fast polypeptide release. The crystal structures of human and
Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the
GTPase domain revealed details of the interaction between these two factors and
marked conformational changes in eRF1 that occur upon binding to eRF3, leading
eRF1 to resemble a tRNA molecule. Small-angle X-ray scattering analysis of the
eRF1/eRF3/GTP complex suggested that eRF1's M domain contacts eRF3's GTPase
domain. Consistently, mutation of Arg192, which is predicted to come in close
contact with the switch regions of eRF3, revealed its important role for eRF1's
stimulatory effect on eRF3's GTPase activity. An ATP molecule used as a
crystallization additive was bound in eRF1's putative decoding area. Mutational
analysis of the ATP-binding site shed light on the mechanism of stop codon
recognition by eRF1.
|
|
|
|
|
|
|
