Author
Listed:
- 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
Technical University of Munich)
- 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
New York State Psychiatric Institute)
- 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
Technical University of Munich)
- Jonathan A. Javitch
(Columbia University
New York State Psychiatric Institute
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)
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.
Suggested Citation
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 & , 2011.
"Crystal structure of a potassium ion transporter, TrkH,"
Nature, Nature, vol. 471(7338), pages 336-340, March.
Handle:
RePEc:nat:nature:v:471:y:2011:i:7338:d:10.1038_nature09731
DOI: 10.1038/nature09731
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