Defining membrane spanning domains and crucial membrane-localized acidic amino acid residues for K+ transport of a Kup/HAK/KT-type Escherichia coli potassium transporter-Reference-Cited by-同舟云学术

Defining membrane spanning domains and crucial membrane-localized acidic amino acid residues for K+ transport of a Kup/HAK/KT-type Escherichia coli potassium transporter

Published:2014-02-11 Issue:5 Volume:155 Page:315-323
ISSN:1756-2651
Container-title:The Journal of Biochemistry
language:en
Short-container-title:

Author:

Sato Yoko,Nanatani Kei,Hamamoto Shin,Shimizu Makoto,Takahashi Miho,Tabuchi-Kobayashi Mayumi,Mizutani Akifumi,Schroeder Julian I.,Souma Satoshi,Uozumi Nobuyuki

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://academic.oup.com/jb/article-pdf/155/5/315/14146448/mvu007.pdf

Reference53 articles.

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2. Prokaryotic Kdp-ATPase: recent insights into the structure and function of KdpB;Haupt;J. Mol. Microbiol. Biotechnol.,2005

3. Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals;Hu;J. Struct. Biol.,2008

4. Nucleotide sequence and 3′-end deletion studies indicate that the K+-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus;Schleyer;J. Bacteriol.,1993

5. A potassium transporter of the yeast Schwanniomyces occidentalis homologous to the Kup system of Escherichia coli has a high concentrative capacity;Banuelos;EMBO J.,1995

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