2GFP

Structure of the Multidrug Transporter EmrD from Escherichia coli

Summary for 2GFP

Entry DOI	10.2210/pdb2gfp/pdb
Descriptor	Multidrug resistance protein D (1 entity in total)
Functional Keywords	membrane protein; multidrug transporter, membrane protein
Biological source	Escherichia coli
Cellular location	Cell inner membrane; Multi-pass membrane protein: P31442
Total number of polymer chains	2
Total formula weight	80027.80
Authors	Yin, Y.,He, X.,Szewczyk, P.,Nguyen, T.,Chang, G. (deposition date: 2006-03-22, release date: 2006-05-16, Last modification date: 2024-02-14)
Primary citation	Yin, Y.,He, X.,Szewczyk, P.,Nguyen, T.,Chang, G. Structure of the multidrug transporter EmrD from Escherichia coli Science, 312:741-744, 2006 Cited by PubMed Abstract: EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity. PubMed: 16675700 DOI: 10.1126/science.1125629 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.5 Å)

Structure validation