Type | Description |
---|---|
Definition | ATP synthase F1 subunit beta |
Date | Results | Publications |
---|---|---|
2016-08-27 12:08:00 | Combining cryoelectron microscopy data with bioinformatic analysis allowed the authors to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. | 26439008 |
2015-05-16 12:04:00 | These data indicate that interaction with the alpha-phosphate is not crucial for efficient catalysis, but likely contributes to avoid formation of ADP-inhibited intermediates. | 25681765 |
2015-05-16 10:53:00 | Molecular dynamics simulations show that the nucleotide-free beta subunit, initially in the open, low-affinity state, undergoes a spontaneous closing transition to the half-open state in response to the gamma rotation in the synthesis direction. | 24798048 |
2012-10-06 11:36:00 | analysis of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria | 22733764 |
2011-10-08 11:47:00 | Molecular dynamics simulations of F1-ATPase suggest that the equilibrium conformation of a nucleotide-free beta-subunit is the open conformation and that the transition from the closed to the open conformation can occur in a few tens of nanoseconds. | 21452901 |
Type | IDs |
---|---|
Synonymous | ATP5B |
Gene |
UniProtKB-ID:
ATPB_BOVIN
UniprotKB:
P00829
UniParc:
UPI000012642B
EMBL:
X05605,
BC116099,
M20929
KO:
bta:327675
|
Nucleutide sequences |
EMBL-CDS:
CAA29094.1,
AAA30395.1,
AAI16100.1
|
Protein sequencees |
RefSeq:
NP_786990.1
|
Others |
UniRef100:
UniRef100_P00829
UniRef90:
UniRef90_P00829
UniRef50:
UniRef50_P00829
UniGene:
Bt.4431
|
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---|---|---|---|---|---|---|---|---|
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