PDBsum entry 2m6l

Transport protein

PDB id: 2m6l

Contents

Protein chain

292 a.a.

PDB id:

2m6l

Name:

Transport protein

Title:

Solution structure of the escherichia coli holo ferric enterobactin binding protein

Structure:

Ferrienterobactin-binding periplasmic protein. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b0592, fepb, jw0584. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

B.C.H.Chu,R.Otten,K.D.Krewulak,F.A.A.Mulder,H.J.Vogel

Key ref:

B.C.Chu et al. (2014). The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB. J Biol Chem, 289, 29219-29234. PubMed id: 25173704 DOI: 10.1074/jbc.M114.564021

Date:

05-Apr-13 Release date: 30-Apr-14

Protein chain

P0AEL6  (FEPB_ECOLI) -  Ferric enterobactin-binding periplasmic protein FepB from Escherichia coli (strain K12)

Seq: 318 a.a.

Struc: 292 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M114.564021

J Biol Chem 289:29219-29234 (2014)

PubMed id: 25173704

The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.

B.C.Chu, R.Otten, K.D.Krewulak, F.A.Mulder, H.J.Vogel.

ABSTRACT

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.