PDBsum entry 4zow

Transport protein

PDB id: 4zow

Contents

Protein chain

391 a.a.

Ligands

CLM

Waters ×13

PDB id:

4zow

Name:

Transport protein

Title:

Crystal structure of e. Coli multidrug transporter mdfa in complex with chloramphenicol

Structure:

Multidrug transporter mdfa. Chain: a. Fragment: unp residues 10-400. Synonym: chloramphenicol resistance pump cmr. Engineered: yes. Mutation: yes

Source:

Escherichia coli (strain k12). Organism_taxid: 83333. Strain: k12. Gene: mdfa, cmla, cmr, b0842, jw0826. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768

Resolution:

2.45Å R-factor: 0.206 R-free: 0.235

Authors:

X.C.Zhang,J.Heng,Y.Zhao,X.Wang

Key ref:

J.Heng et al. (2015). Substrate-bound structure of the E. coli multidrug resistance transporter MdfA. Cell Res, 25, 1060-1073. PubMed id: 26238402 DOI: 10.1038/cr.2015.94

Date:

07-May-15 Release date: 19-Aug-15

Protein chain

P0AEY8  (MDFA_ECOLI) -  Multidrug transporter MdfA from Escherichia coli (strain K12)

Seq: 410 a.a.

Struc: 391 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/cr.2015.94

Cell Res 25:1060-1073 (2015)

PubMed id: 26238402

Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.

J.Heng, Y.Zhao, M.Liu, Y.Liu, J.Fan, X.Wang, Y.Zhao, X.C.Zhang.

ABSTRACT

Multidrug resistance is a serious threat to public health. Proton motive force-driven antiporters from the major facilitator superfamily (MFS) constitute a major group of multidrug-resistance transporters. Currently, no reports on crystal structures of MFS antiporters in complex with their substrates exist. The E. coli MdfA transporter is a well-studied model system for biochemical analyses of multidrug-resistance MFS antiporters. Here, we report three crystal structures of MdfA-ligand complexes at resolutions up to 2.0 Å, all in the inward-facing conformation. The substrate-binding site sits proximal to the conserved acidic residue, D34. Our mutagenesis studies support the structural observations of the substrate-binding mode and the notion that D34 responds to substrate binding by adjusting its protonation status. Taken together, our data unveil the substrate-binding mode of MFS antiporters and suggest a mechanism of transport via this group of transporters.