EC Number   |
Protein Variants |
Reference |
|---|
   7.6.2.8 | D141C |
site-directed mutagenesis of BtuF on a residue pointing outward in the middle of the alpha-helix connecting the two lobes, the mutation allows for specific coupling of fluorescent labels to each of these proteins |
751661 |
| 7.6.2.8 | E159Q |
mutation in subunit BtuD, results in abolished ATP hydrolysis activity of BtuCDF. Mutant is still able to bind nucleotides and binding protein BtuF in a manner similar to the wild-type protein |
719509 |
| 7.6.2.8 | E159Q |
site-directed mutagenesis of BtuD, an ATPase impaired mutant |
751661 |
| 7.6.2.8 | E159Q/N162C |
site-directed mutagenesis, a disulfide mutant, analysis of the crystal structure of the mutant with bound ATP |
750063 |
| 7.6.2.8 | E159Q/N162C |
the mutant is unable to transport substrate despite a very low residual ATP hydrolysis rate |
734771 |
| 7.6.2.8 | E159Q/N162C |
the mutant shows dramatically reduced ATPase activity |
734760 |
| 7.6.2.8 | L85C |
the mutant shows a 6.5fold reduction in ATPase activity compared to the wild type enzyme |
734771 |
| 7.6.2.8 | more |
a system consisting of the BtuC subunit embedded in a palmitoyloleoyl phosphatidylcholine lipid bilayer is constructed and a more-than-57ns MD simulation is performed to study the functional motions of BtuC at the atomic level: results show that a stable protein-lipid bilayer is obtained and the palmitoyloleoyl phosphatidylcholine lipid bilayer is able to adjust its thickness to match the embedded BtuC which undergo relatively complicated motions |
713505 |
| 7.6.2.8 | more |
generation of chimeric ABCD4 proteins that are exchanged in terms of the corresponding putative transmembrane helix with ABCD1 (based on the secondary structure of the eukaryotic P-glycoprotein homolog CmABCB1) in HEK-293 cells, endogenous human ABCD1 does not interact with LMBD1. Construction of ABCD4 chimeras 1-6 and analysis of the localization of chimeric ABCD4s in CHO cells stably expressing LMBD1-GFP. The wild-type ABCD4 co-expressed with LMBD1 exhibits a punctate distribution that is superimposable on the distribution pattern of LMBD1. The distribution patterns of the ABCD4 chimeras 1, 3, 4 and 6 also display the same pattern as LMBD1. But ABCD4 chimeras 2 and 5 do not exhibit a punctate pattern, but rather, a reticulum-like distribution pattern that is not superimposable on LMBD1 |
752200 |
| 7.6.2.8 | more |
site-directed mutagenesis of tryptophan residue W66 in the substrate binding cleft , the affinity for cobinamide of the W66X mutants is lower except for W66F. Three mutants with impaired Cbi binding (W66A, W66R, and W66E) and one with high binding affinity (W66F) are used for transport assays. Despite having lower Cbi binding affinities, Cbi transport is hardly affected by W66X substitution |
752221 |
