6IDR

Crystal structure of Vibrio cholerae MATE transporter VcmN in the bent form

Summary for 6IDR

• Entry DOI: 10.2210/pdb6idr/pdb
• Descriptor: MATE family efflux transporter, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total)
• Functional Keywords: mate multidrug transporter, transport protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 1
• Total formula weight: 48949.69

Authors

Kusakizako, T.,Claxton, D.P.,Tanaka, Y.,Maturana, A.D.,Kuroda, T.,Ishitani, R.,Mchaourab, H.S.,Nureki, O. (deposition date: 2018-09-11, release date: 2019-01-16, Last modification date: 2024-03-27)

Primary citation

Kusakizako, T.,Claxton, D.P.,Tanaka, Y.,Maturana, A.D.,Kuroda, T.,Ishitani, R.,Mchaourab, H.S.,Nureki, O.
Structural Basis of H+-Dependent Conformational Change in a Bacterial MATE Transporter.
Structure, 27:293-, 2019

PubMed Abstract: Multidrug and toxic compound extrusion (MATE) transporters efflux toxic compounds using a Na or H gradient across the membrane. Although the structures of MATE transporters have been reported, the cation-coupled substrate transport mechanism remains controversial. Here we report crystal structures of VcmN, a Vibrio cholerae MATE transporter driven by the H gradient. High-resolution structures in two distinct conformations associated with different pHs revealed that the rearrangement of the hydrogen-bonding network around the conserved Asp35 induces the bending of transmembrane helix 1, as in the case of the H-coupled Pyrococcus furiosus MATE transporter. We also determined the crystal structure of the D35N mutant, which captured a unique conformation of TM1 facilitated by an altered hydrogen-bonding network. Based on the present results, we propose a common step in the transport cycle shared among prokaryotic H-coupled MATE transporters.

PubMed: 30449688
DOI: 10.1016/j.str.2018.10.004

Experimental method

X-RAY DIFFRACTION (2.502 Å)