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Author(s): Vieira-Pires, RS
Szollosi, A
Morais-Cabral, JH
Title: The structure of the KtrAB potassium transporter
Publisher: Nature Publishing Group
Issue Date: 2013
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.
Subject: Adenosine Diphosphate/metabolism
Adenosine Triphosphate/metabolism
Bacillus subtilis/chemistry
Bacterial Proteins/chemistry
Bacterial Proteins/metabolism
Cation Transport Proteins/chemistry
Cation Transport Proteins/metabolism
Crystallography, X-Ray
Ion Transport
Models, Biological
Models, Molecular
Protein Conformation
Protein Subunits/chemistry
Protein Subunits/metabolism
Structure-Activity Relationship
Source: Nature, vol. 496(7445), p. 323-8
Related Information: info:eu-repo/grantAgreement/FCT/5876-PPCDTI/99861/PT
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
Appears in Collections:I3S - Artigo em Revista Científica Internacional

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