Why WrbA is weaker than flavodoxin in binding FMN. A molecular modeling study

Hong Fang Ji, Liang Shen, Jannette Carey, Rita Grandori, Hong Yu Zhang

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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 is predicted to share the twisted α/β open-sheet fold of the flavodoxins and to bind flavin mononucleotide (FMN) as its physiological cofactor, the binding is much weaker in comparison with flavodoxin (the binding constants are ∼2 μM for WrbA and ∼1 nM for flavodoxin). To elucidate the different FMN-binding behaviors of WrbA and flavodoxin, we modeled the WrbA structure and examined its interactions with FMN by docking experiments, and then compared them with those at the flavodoxin active site. The results provide a rationale for the reduced cofactor affinity displayed by WrbA relative to flavodoxin.

Original languageEnglish (US)
Pages (from-to)155-160
Number of pages6
JournalJournal of Molecular Structure: THEOCHEM
Volume764
Issue number1-3
DOIs
StatePublished - May 30 2006

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

Keywords

  • Docking calculations
  • Homology modeling
  • Hydrogen bonds
  • Hydrophobic interactions
  • Protein evolution

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