The structure of the KtrAB potassium transporter.

Abstract:

:In bacteria, archaea, fungi and plants the Trk, Ktr and HKT ion transporters are key components of osmotic regulation, pH homeostasis and resistance to drought and high salinity. These ion transporters are functionally diverse: they can function as Na(+) or K(+) channels and possibly as cation/K(+) symporters. They are closely related to potassium channels both at the level of the membrane protein and at the level of the cytosolic regulatory domains. Here we describe the crystal structure of a Ktr K(+) transporter, the KtrAB complex from Bacillus subtilis. The structure shows the dimeric membrane protein KtrB assembled with a cytosolic octameric KtrA ring bound to ATP, an activating ligand. A comparison between the structure of KtrAB-ATP and the structures of the isolated full-length KtrA protein with ATP or ADP reveals a ligand-dependent conformational change in the octameric ring, raising new ideas about the mechanism of activation in these transporters.

journal_name

Nature

journal_title

Nature

authors

Vieira-Pires RS,Szollosi A,Morais-Cabral JH

doi

10.1038/nature12055

subject

Has Abstract

pub_date

2013-04-18 00:00:00

pages

323-8

issue

7445

eissn

0028-0836

issn

1476-4687

pii

nature12055

journal_volume

496

pub_type

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