When biochemistry meets structural biology: the cautionary tale of EmrE.
When biochemistry meets structural biology a more complete understanding of the mechanism of biological macromolecules is usually achieved. Several high-resolution structures of ion-coupled transporters have enriched the understanding of mechanisms of substrate recognition, translocation and coupling of substrate fluxes. However, two X-ray structures of EmrE, the smallest ion-coupled multi-drug transporter, raised questions over the veracity of the structural model and represented a cautionary tale about the difficulty of determining the 3D structures of membrane proteins and the dangers of ignoring biochemical results. The 3D structures of EmrE have since been retracted because of faulty software, but the suggestion that the protomers in the dimer are in an antiparallel topological orientation sparked controversy that is still ongoing.
Schuldiner
Shimon
S
Department of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel. Shimon.Schuldiner@huji.ac.il
D017920:Antiporters / Q000737:chemistry* / Q000187:drug effects; D018360:Crystallography, X-Ray; D003902:Detergents / Q000494:pharmacology; D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000187:drug effects; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D017433:Protein Structure, Secondary / Q000187:drug effects; D012180:Retraction of Publication as Topic; D012984:Software
D017920:Antiporters; D003902:Detergents; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C075436:EmrE protein, E coli