4LZ6

Structure of MATE multidrug transporter DinF-BH

Summary for 4LZ6

• Entry DOI: 10.2210/pdb4lz6/pdb
• Related: 4LZ9
• Descriptor: BH2163 protein (1 entity in total)
• Functional Keywords: multidrug transporter, transport protein
• Biological source: Bacillus halodurans
• Total number of polymer chains: 1
• Total formula weight: 48615.17

Authors

Lu, M.,Radchenko, M.,Symersky, J.,Nie, R.,Guo, Y. (deposition date: 2013-07-31, release date: 2013-10-23, Last modification date: 2024-03-20)

Primary citation

Lu, M.,Radchenko, M.,Symersky, J.,Nie, R.,Guo, Y.
Structural insights into H(+)-coupled multidrug extrusion by a MATE transporter
Nat.Struct.Mol.Biol., 20:1310-1317, 2013

PubMed Abstract: Multidrug and toxic compound extrusion (MATE) transporters contribute to multidrug resistance by coupling the efflux of drugs to the influx of Na(+) or H(+). Known structures of Na(+)-coupled, extracellular-facing MATE transporters from the NorM subfamily revealed 12 membrane-spanning segments related by a quasi-two-fold rotational symmetry and a multidrug-binding cavity situated near the membrane surface. Here we report the crystal structure of an H(+)-coupled MATE transporter from Bacillus halodurans and the DinF subfamily at 3.2-Å resolution, unveiling a surprisingly asymmetric arrangement of 12 transmembrane helices. We also identified a membrane-embedded substrate-binding chamber by combining crystallographic and biochemical analyses. Our studies further suggested a direct competition between H(+) and substrate during DinF-mediated transport and implied how a MATE transporter alternates between its extracellular- and intracellular-facing conformations to propel multidrug extrusion. Collectively, our results demonstrated heretofore-unrecognized mechanistic diversity among MATE transporters.

PubMed: 24141706
DOI: 10.1038/nsmb.2687

Experimental method

X-RAY DIFFRACTION (3.2 Å)