The protein WrbA from Escherichia coli is the founding member of a class of novel multimeric flavodoxin-like proteins implicated in defense against oxidative stress. Although WrbA proteins share the twisted ¿/¿ open-sheet fold of the flavodoxins and binds flavin mononucleotide (FMN) as its physiological cofactor, FMN binding is much weaker in comparison with flavodoxin (Kd ~2¿¿M for E. coli WrbA and ~1 nM for flavodoxins). To elucidate the different FMN-binding behaviors of WrbA and flavodoxin, we modeled the E. coli WrbA structure and examined its interactions with FMN by docking experiments, and compared the results with the flavodoxin active site. The results suggest an explanation for the reduced cofactor affinity displayed by WrbA relative to flavodoxin.
Ji, H., Shen, L., Carey, J., Grandori, R., Zhang, H. (2006). Why WrbA is weaker than flavodoxin in binding FMN. A molecular modeling study. JOURNAL OF MOLECULAR STRUCTURE. THEOCHEM, 764(1-3), 155-160 [10.1016/j.theochem.2006.01.027].
Why WrbA is weaker than flavodoxin in binding FMN. A molecular modeling study
GRANDORI, RITA;
2006
Abstract
The protein WrbA from Escherichia coli is the founding member of a class of novel multimeric flavodoxin-like proteins implicated in defense against oxidative stress. Although WrbA proteins share the twisted ¿/¿ open-sheet fold of the flavodoxins and binds flavin mononucleotide (FMN) as its physiological cofactor, FMN binding is much weaker in comparison with flavodoxin (Kd ~2¿¿M for E. coli WrbA and ~1 nM for flavodoxins). To elucidate the different FMN-binding behaviors of WrbA and flavodoxin, we modeled the E. coli WrbA structure and examined its interactions with FMN by docking experiments, and compared the results with the flavodoxin active site. The results suggest an explanation for the reduced cofactor affinity displayed by WrbA relative to flavodoxin.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.