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Results 1 - 10 of 11 > >>
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Reference
-999
-
crystal structure of BtuCD-F complex presented, displacement of vitamin B12 from binding pocket shown, subunits of transmembrane BtuC protein shown to have two distinct conformations, translocation pathway shown to be closed to both sides of the membrane, electron paramagnetic resonance spectra of spin-labeled cysteine mutants shown to be consistent with the conformation of BtuCD-F observed in the crystal structure, structure of BtuCD-F discussed as a posttranslocation intermediate
-999
-
intrinsic flexibility of isolated BtuC and BtuD dimers evaluated, conformational movement of intact BtuCD transporter studied in the context of conformational coupling between BtuC and BtuD, effect of BtuF association on the transporter conformational movement discussed
-999
-
perturbed anisotropic network model and molecular dynamics simulations applied, essential dynamics sampling and cavity and pathway analysis, structural response of BtuC protein quantified in terms of X-shifts shown, transport model discussed
-999
-
principal motions and conformational changes of apo and holo forms studied, closed conformation for the ligand-bound state identified, empty form shown to fluctuate between open and closed conformations, simulation system and force field parameters described, elastic network normal-mode analysis performed, conformational changes summarized, domain motions indicated, link to previous simulations and biological implications discussed
-999
-
principal motions of BtuCD-F transporter system and conformation of ATP-binding sites analyzed, protein subunits representing simulation components indicated, design of simulation system described, conformational drift summarized, model of the BtuCD-F complex discussed
-999
-
steered molecular dynamics simulations performed, principal component analysis and energetics of vitamin B12 unbinding analyzed, potential of mean force along postulated vitamin B12 unbinding pathway constructed through Jarzynski's equality, motion modes and intrinsic flexibility of BtuF calculated, Trp44-Gln45 pair situated at binding pocket suggested to act as a gate in the vitamin B12 binding and unbinding process
-999
-
vitamin B12 has little effect on the activity in proteoliposomes, as well as in the presence of lauryl dimethylamine-N-oxide, dodecyl maltoside and Triton X-100
0.18
-
in the absence of Btu-F and vitamin B12 in proteoliposomes
0.33
-
in the presence of Fos-choline
0.44
-
in the presence of 0.02 mmol BtuF in proteoliposomes
Results 1 - 10 of 11 > >>