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 Jiang and Ming Zhou ()
Additional contact information
Yu Cao: College of Physicians and Surgeons, Columbia University
Xiangshu Jin: Center for Computational Biology and Bioinformatics, Howard Hughes Medical Institute, Columbia University
Hua Huang: College of Physicians and Surgeons, Columbia University
Mehabaw Getahun Derebe: University of Texas Southwestern Medical Center
Elena J. Levin: College of Physicians and Surgeons, Columbia University
Venkataraman Kabaleeswaran: College of Physicians and Surgeons, Columbia University
Yaping Pan: College of Physicians and Surgeons, Columbia University
Marco Punta: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
James Love: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Jun Weng: College of Physicians and Surgeons, Columbia University
Matthias Quick: Columbia University
Sheng Ye: University of Texas Southwestern Medical Center
Brian Kloss: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Renato Bruni: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Erik Martinez-Hackert: Howard Hughes Medical Institute, Columbia University
Wayne A. Hendrickson: Howard Hughes Medical Institute, Columbia University
Burkhard Rost: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Jonathan A. Javitch: Columbia University
Kanagalaghatta R. Rajashankar: Cornell University, NE-CAT, Advanced Photon Source
Youxing Jiang: University of Texas Southwestern Medical Center
Ming Zhou: College of Physicians and Surgeons, Columbia University

Nature, 2011, vol. 471, issue 7338, 336-340

Abstract: Abstract 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.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature09731 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:471:y:2011:i:7338:d:10.1038_nature09731

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature09731

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().