Affiliation:
1. Abteilung Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, D-49069 Osnabrück, Germany
Abstract
ABSTRACT
When grown under conditions of potassium limitation or high osmolality,
Escherichia coli
synthesizes the K
+
-translocating KdpFABC complex. The KdpA subunit, which has sequence homology to potassium channels of the KcsA type, has been shown to be important for potassium binding and transport. Replacement of the glycine residues in KdpA at positions 345 and 470, members of putative selectivity filter regions III and IV, alters the ion selectivity of the KdpFABC complex.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference19 articles.
1. Altendorf K. and W. Epstein. 1996. The Kdp-ATPase of Escherichia coli p. 403-420. In A. G. Lee (ed.) Biomembranes (ATPases) vol. 5. JAI Press Inc. London England.
2. Altendorf, K., M. Gaβel, W. Puppe, T. Möllenkamp, A. Zeeck, C. Boddien, K. Fendler, E. Bamberg, and S. Dröse. 1998. Structure and function of the Kdp-ATPase of Escherichia coli. Acta Physiol. Scand.163:137-146.
3. Buurman, E. T., K.-T. Kim, and W. Epstein. 1995. Genetic evidence of two sequentially occupied K+ binding sites in the Kdp transport ATPase. J. Biol. Chem.270:6678-6685.
4. Dorus, S., H. Mimura, and W. Epstein. 2001. Substrate-binding clusters of the K+-transporting Kdp ATPase of Escherichia coli investigated by amber suppression scanning mutagenesis. J. Biol. Chem.276:9590-9598.
5. Doyle, D. A., J. M. Cabral, R. A. Pfuetzner, A. Kuo, J. M. Gulbis, S. L. Cohen, B. T. Chait, and R. MacKinnon. 1998. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science280:69-77.
Cited by
27 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献