Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity.
about
A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids.Mutants of EF-Tu defective in binding aminoacyl-tRNA.The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.
P2860
Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Histidine-118 of elongation fa ...... lation of the GTPase activity.
@en
type
label
Histidine-118 of elongation fa ...... lation of the GTPase activity.
@en
prefLabel
Histidine-118 of elongation fa ...... lation of the GTPase activity.
@en
P2093
P2860
P1433
P1476
Histidine-118 of elongation fa ...... lation of the GTPase activity.
@en
P2093
Anborgh PH
Parmeggiani A
P2860
P356
10.1016/0014-5793(94)80614-4
P407
P577
1994-04-01T00:00:00Z