KdpFABC Reconstituted in Escherichia coli Lipid Vesicles: Substrate Dependence of the Transport Rate
Author:
Affiliation:
1. Department of Biology and Konstanz Research School Chemical Biology, University of Konstanz, 78464 Konstanz, Germany
Funder
Graduiertenschule Chemische Biologie, Universität Konstanz
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi5008244
Reference31 articles.
1. Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex fromEscherichia coli(Review)
2. Structural similarities of Na,K-ATPase and SERCA, the Ca2+-ATPase of the sarcoplasmic reticulum
3. Characterization of Amino Acid Substitutions in KdpA, the K + -Binding and -Translocating Subunit of the KdpFABC Complex of Escherichia coli
4. The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone
5. The KdpF Subunit Is Part of the K+-translocating Kdp Complex of Escherichia coli and Is Responsible for Stabilization of the Complex in Vitro
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