ABCC8 p.Phe48Arg
| Predicted by SNAP2: | A: N (53%), C: N (66%), D: D (71%), E: D (53%), G: D (59%), H: D (53%), I: N (78%), K: D (66%), L: N (82%), M: N (72%), N: D (63%), P: D (71%), Q: D (53%), R: D (66%), S: N (53%), T: N (61%), V: N (57%), W: N (53%), Y: N (57%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, G: D, H: D, I: N, K: D, L: N, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, V: N, W: D, Y: N, |
[switch to compact view]
Comments [show]
None has been submitted yet.
[hide] Investigation of the role of a surface patch in th... Biochim Biophys Acta. 1999 Aug 17;1433(1-2):159-69. Couture MM, Auger M, Rosell F, Mauk AG, Boubour E, Lennox RB, Eltis LD
Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein.
Biochim Biophys Acta. 1999 Aug 17;1433(1-2):159-69., [PMID:10446369]
Abstract [show]
The role of a flattened, relatively hydrophobic surface patch in the self-association of Chromatium vinosum HiPIP was assessed by substituting phenylalanine 48 with lysine. The reduction potential of the F48K variant was 26 mV higher than that of the wild-type (WT) recombinant (rc) HiPIP, consistent with the introduction of a positive charge close to the cluster. Nuclear magnetic resonance spectroscopy (NMR) revealed that the electronic structure of the oxidized cluster in these two proteins is very similar at 295 K. In contrast, the electron transfer self-exchange rate constant of F48K was at least 15-fold lower than that of the WT rcHiPIP, indicating that the introduction of a positive charge at position 48 diminishes self-association of the HiPIP in solution. Moreover, the substitution at position 48 abolished the fine structure in the g(z) region of the electron paramagnetic resonance (EPR) spectrum of oxidized C. vinosum rcHiPIP recorded in the presence of 1 M sodium chloride. These results support the hypothesis that the flattened, relatively hydrophobic patch mediates interaction between two molecules of HiPIP and that freezing-induced dimerization of the HiPIP mediated by this patch is responsible for the unusual fine structure observed in the EPR spectrum of the oxidized C. vinosum HiPIP.
Comments [show]
None has been submitted yet.
No. Sentence Comment
124 For example, the reduction potentials of the F48R variant C. vinosum HiPIP was 23 mV higher than that of the WT [31] and that of the V66K variant Ectothiorhodospira halophila HiPIP was 29 mV higher than that of the WT [32].
X
ABCC8 p.Phe48Arg 10446369:124:45
status: NEW141 The 1 H-NMR spectrum of oxidized C. vinosum F48K rcHiPIP is very similar to that of the F48R variant [31].
X
ABCC8 p.Phe48Arg 10446369:141:88
status: NEW162 Interestingly, the electron transfer self-exchange of F48R variant C. vinosum HiPIP has been calculated by EXSY to be one third of the kex calculated for the WT [31].
X
ABCC8 p.Phe48Arg 10446369:162:54
status: NEW