10.5452/MA-AQ91Z
Crouzy, Serge
FUR dimer Escherichia coli
modelarchive.org
2015
3D macromolecular model
2015-09-08
en
ABSTRACT
The FUR protein (Ferric Uptake Regulator) is an iron-dependent global transcriptional regulator. Specific to bacteria, FUR is an attractive antibacterial target since virulence is correlated to iron bioavailability.
No complete experimental structure of FUR from Escherichia coli is available to date.
Here, a model of EcFUR dimer from residue 2 to 134 is built by homology from FUR vibrio cholerae (more than 80% similar residues). Model is refined by energy minimization with the CHARMM molecular mechanics force field in implicit solvent. Model is validated in two ways : i) both monomers superimpose very well with the known crystal structure of the N-terminal domain (2FU4) ii) Docking of inhibitor peptides to the EcFUR model dimer agree with in vitro assays. The model includes 4 Fe2+ and 2 Zn2+ metal ions in their putative respective binding sites.