2m6l | pdb_00002m6l

Solution structure of the Escherichia coli holo ferric enterobactin binding protein

spinqualitylabelsall models 2m6l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m6l is a 1 chain structure with sequence from Escherichia coli K-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FEPB_ECOLI Binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin. Publication Abstract from PubMed The periplasmic binding protein (PBP) FepB plays a key role in transporting the catecholate siderophore ferric enterobactin from the outer to the inner membrane in Gram-negative bacteria. The solution structures of the 34-kDa apo- and holo-FepB from Escherichia coli, solved by NMR, represent the first solution structures determined for the type III class of PBPs. Unlike type I and II PBPs, which undergo large "Venus flytrap" conformational changes upon ligand binding, both forms of FepB maintain similar overall folds; however, binding of the ligand is accompanied by significant loop movements. Reverse methyl cross-saturation experiments corroborated chemical shift perturbation results and uniquely defined the binding pocket for gallium enterobactin (GaEnt). NMR relaxation experiments indicated that a flexible loop (residues 225-250) adopted a more rigid and extended conformation upon ligand binding, which positioned residues for optimal interactions with the ligand and the cytoplasmic membrane ABC transporter (FepCD), respectively. In conclusion, this work highlights the pivotal role that structural dynamics plays in ligand binding and transporter interactions in type III PBPs. The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.,Chu BC, Otten R, Krewulak KD, Mulder FA, Vogel HJ J Biol Chem. 2014 Oct 17;289(42):29219-34. doi: 10.1074/jbc.M114.564021. Epub, 2014 Aug 29. PMID:25173704 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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