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PDBsum entry 4zp0

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Transport protein PDB id
4zp0
Contents
Protein chain
392 a.a.
Ligands
DXC
LDA ×2
Waters ×18

References listed in PDB file
Key reference
Title Substrate-Bound structure of the e. Coli multidrug resistance transporter mdfa.
Authors J.Heng, Y.Zhao, M.Liu, Y.Liu, J.Fan, X.Wang, Y.Zhao, X.C.Zhang.
Ref. Cell Res, 2015, 25, 1060-1073. [DOI no: 10.1038/cr.2015.94]
PubMed id 26238402
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.
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