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.
Articolo in rivista - Articolo scientifico
homology modeling, docking calculations, protein evolution, hydrogen bonds, hydrophobic interactions.
English
30-mag-2006
764
1-3
155
160
none
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].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/2348
Citazioni
  • Scopus 5
  • ???jsp.display-item.citation.isi??? 5
Social impact