› 2i68

Electron crystallography
7.5Å resolution

Cryo-EM based theoretical model structure of transmembrane domain of the multidrug-resistance antiporter from E. coli EmrE

Released:
DOI: 10.2210/pdb2i68/pdb
PDB entry 2i68 coloured by chain, front view.
PDB entry 2i68 coloured by chain, side view.
PDB entry 2i68 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain.
Fleishman SJ, Harrington SE, Enosh A, Halperin D, Tate CG, Ben-Tal N
J Mol Biol 364 54-67 (2006)
PMID: 17005200
Related structures: EMD-1087

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150097 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug transporter EmrE Chains: A, B
Molecule details ›
Chains: A, B
Length: 137 amino acids
Theoretical weight: 15.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P23895 (Residues: 1-110; Coverage: 100%)
Gene names: JW0531, b0543, eb, emrE, mvrC
Sequence domains: Small Multidrug Resistance protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.5Å
Relevant EMDB volumes: EMD-1087
Expression system: Escherichia coli

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Citations

15 review citations

Multidrug resistance in bacteria.
Nikaido H. (2009)
14 more

12 mentions without citation

Advances in structural and functional analysis of membrane proteins by electron crystallography.
Wisedchaisri et al. (2011)
11 more