Crystal structure of a potassium ion transporter, TrkH

Yu Cao, Xiangshu Jin, Hua Huang, Mehabaw Getahun Derebe, Elena J. Levin, Venkataraman Kabaleeswaran, Yaping Pan, Marco Punta, James Love, Jun Weng, Matthias Quick, Sheng Ye, Brian Kloss, Renato Bruni, Erik Martinez-Hackert, Wayne A. Hendrickson, Burkhard Rost, Jonathan A. Javitch, Kanagalaghatta R. Rajashankar, Youxing JiangMing Zhou

Research output: Contribution to journalArticlepeer-review

110 Scopus citations


The TrkH/TrkG/KtrB proteins mediate K+ uptake in bacteria and probably evolved from simple K+ channels by multiple gene duplications or fusions. Here we present the crystal structure of a TrkH from Vibrio parahaemolyticus. TrkH is a homodimer, and each protomer contains an ion permeation pathway. A selectivity filter, similar in architecture to those of K+ channels but significantly shorter, is lined by backbone and side-chain oxygen atoms. Functional studies showed that TrkH is selective for permeation of K+ and Rb + over smaller ions such as Na + or Li +. Immediately intracellular to the selectivity filter are an intramembrane loop and an arginine residue, both highly conserved, which constrict the permeation pathway. Substituting the arginine with an alanine significantly increases the rate of K+ flux. These results reveal the molecular basis of K + selectivity and suggest a novel gating mechanism for this large and important family of membrane transport proteins.

Original languageEnglish (US)
Pages (from-to)336-341
Number of pages6
Issue number7338
StatePublished - Mar 17 2011

ASJC Scopus subject areas

  • General


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