Skip to main content
Kent Academic Repository

Family resemblances: A common fold for some dimeric ion-coupled secondary transporters

Vergara-Jaque, Ariela, Fenollar-Ferrer, Cristina, Mulligan, Christopher, Mindell, Joseph A, Forrest, Lucy R (2015) Family resemblances: A common fold for some dimeric ion-coupled secondary transporters. The Journal of General Physiology, 146 (5). pp. 423-434. ISSN 0022-1295. (doi:10.1085/jgp.201511481) (KAR id:61673)


Membrane transporter proteins catalyze the passage of a broad range of solutes across cell membranes, allowing the uptake and efflux of crucial compounds. Because of the difficulty of expressing, purifying, and crystallizing integral membrane proteins, relatively few transporter structures have been elucidated to date. Although every membrane transporter has unique characteristics, structural and mechanistic similarities between evolutionarily diverse transporters have been identified. Here, we compare two recently reported structures of membrane proteins that act as antimicrobial efflux pumps, namely MtrF from Neisseria gonorrhoeae and YdaH from Alcanivorax borkumensis, both with each other and with the previously published structure of a sodium-dependent dicarboxylate transporter from Vibrio cholerae, VcINDY. MtrF and YdaH belong to the p-aminobenzoyl-glutamate transporter (AbgT) family and have been reported as having architectures distinct from those of all other families of transporters. However, our comparative analysis reveals a similar structural arrangement in all three proteins, with highly conserved secondary structure elements. Despite their differences in biological function, the overall "design principle" of MtrF and YdaH appears to be almost identical to that of VcINDY, with a dimeric quaternary structure, helical hairpins, and clear boundaries between the transport and scaffold domains. This observation demonstrates once more that the same secondary transporter architecture can be exploited for multiple distinct transport modes, including cotransport and antiport. Based on our comparisons, we detected conserved motifs in the substrate-binding region and predict specific residues likely to be involved in cation or substrate binding. These findings should prove useful for the future characterization of the transport mechanisms of these families of secondary active transporters.

Item Type: Article
DOI/Identification number: 10.1085/jgp.201511481
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Christopher Mulligan
Date Deposited: 10 May 2017 13:57 UTC
Last Modified: 06 Feb 2020 04:16 UTC
Resource URI: (The current URI for this page, for reference purposes)

University of Kent Author Information

Mulligan, Christopher.

Creator's ORCID:
CReDIT Contributor Roles:
  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.