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PDBsum entry 4zp2
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Transport protein
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PDB id
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4zp2
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PDB id:
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| Name: |
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Transport protein
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Title:
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Crystal structure of e. Coli multidrug transporter mdfa in complex with n-dodecyl-n,n-dimethylamine-n-oxide
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Structure:
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Multidrug transporter mdfa. Chain: a. Fragment: unp residues 9-400. Synonym: chloramphenicol resistance pump cmr. Engineered: yes. Mutation: yes
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Source:
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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
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Resolution:
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2.20Å
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R-factor:
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0.208
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R-free:
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0.232
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Authors:
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X.C.Zhang,J.Heng,Y.Zhao,X.Wang
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Key ref:
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J.Heng
et al.
(2015).
Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.
Cell Res,
25,
1060-1073.
PubMed id:
DOI:
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Date:
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07-May-15
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Release date:
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19-Aug-15
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PROCHECK
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Headers
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References
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P0AEY8
(MDFA_ECOLI) -
Multidrug transporter MdfA from Escherichia coli (strain K12)
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Seq:
Struc:
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410 a.a.
392 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Cell Res
25:1060-1073
(2015)
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PubMed id:
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Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.
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J.Heng,
Y.Zhao,
M.Liu,
Y.Liu,
J.Fan,
X.Wang,
Y.Zhao,
X.C.Zhang.
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ABSTRACT
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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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