Type | Description |
---|---|
Definition | elongation factor Tu |
Date | Results | Publications |
---|---|---|
2017-12-02 11:10:00 | Authors studied the transition between the pre- and post-hydrolysis structures through two distinct pathways and show that the transition free energy is minimal along a non-intuitive pathway that involves "separation" of the GTP binding domain (domain 1) from the OB folds (domains 2 and 3), followed by domain 1 rotation, and, eventually, locking the EF-Tu conformation in the post-hydrolysis state. | 29045140 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
EFTU_ECO57
UniprotKB:
P0A6N3
UniParc:
UPI0000110FB2
EMBL:
BA000007,
AE005174
EnsemblGenome:
Z5553,
BAB37613,
BAB38326,
Z4697
KO:
ece:Z5553,
ecs:ECs4903,
ece:Z4697,
ecs:ECs4190
|
Nucleutide sequences |
EMBL-CDS:
AAG59176.1,
AAG58446.1,
BAB37613.1,
BAB38326.1
EnsemblGenome_TRS:
AAG59176,
BAB38326,
AAG58446,
BAB37613
|
Protein sequencees |
EnsemblGenome_PRO:
BAB38326,
AAG59176,
BAB37613,
AAG58446
RefSeq:
NP_312930.1
|
Others |
UniRef100:
UniRef100_P14647
UniRef90:
UniRef90_P14647
UniRef50:
UniRef50_P14647
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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