Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli.

@article{Gassel2001AnalysisOK,
  title={Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli.},
  author={M. Gassel and K. Altendorf},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 6},
  pages={
          1772-81
        }
}
The Kdp complex, a high affinity ATP-driven K(+) transport system of Escherichia coli, is composed of the four membrane-bound subunits KdpF, KdpA, KdpB and KdpC. Whereas the role of KdpB (catalytical subunit), KdpA (K(+)-translocating subunit) and KdpF (stabilizing peptide) is well understood, the function of KdpC is still unknown. Therefore, a kdpC deletion strain was constructed and complementation experiments were performed using different kdpC constructs. Truncations of the kdpC gene… Expand
A chimeric Anabaena/Escherichia coli KdpD protein (Anacoli KdpD) functionally interacts with E. coli KdpE and activates kdp expression in E. coli
TLDR
The data demonstrate that Anabaena KdpD can interact with the E. coli KDPD C-terminal domain resulting in a protein that is functional in vitro as well as in vivo. Expand
Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase.
TLDR
Various mechanistic pump cycle models were derived from the general Post-Albers scheme of P-type ATPases and discussed in the framework of the experimental evidence to propose a possible molecular pump cycle for KdpFABC. Expand
Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis.
The K+-translocating KdpFABC complex from Escherichia coli functions as a high affinity potassium uptake system and belongs to the superfamily of P-type ATPases, although it exhibits some uniqueExpand
The KdpFABC complex from Escherichia coli: a chimeric K+ transporter merging ion pumps with ion channels.
  • J. Greie
  • Chemistry, Medicine
  • European journal of cell biology
  • 2011
TLDR
The KdpFABC complex represents a multi-subunit ATP-driven potassium pump, which is only found in bacteria and archaea and comprises structural as well as functional homologies to potassium channels of the MPM-type. Expand
The KdpFABC complex – K+ transport against all odds
TLDR
Evidence supporting contradictory models of the KdpFABC complex is discussed and key experiments are identified needed to resolve discrepancies and produce a unified model for this fascinating mechanistic hybrid. Expand
Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals.
TLDR
The utility of electron tomography in structure determination of ordered assemblies, especially when disorder is severe enough to hamper conventional crystallographic analysis, is illustrated. Expand
The K+-translocating KdpFABC complex from Escherichia coli: A P-type ATPase with unique features
TLDR
The latest results are in favor of the notion that KdpC might act as a catalytical chaperone, which cooperatively interacts with the nucleotide to be hydrolyzed and, thus, increases the rather untypical weak nucleotide binding affinity of the KdpB nucleotidebinding domain. Expand
The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress.
TLDR
It is demonstrated that the universal stress protein UspC acts as a scaffolding protein of the KDPD/KdpE signaling cascade by interacting with a Usp domain in KdpD of the UspA subfamily under salt stress. Expand
Prokaryotic Kdp-ATPase: Recent Insights into the Structure and Function of KdpB
TLDR
It can be concluded that KdpB is currently misgrouped as class IA because of the conserved 395KGXXD/E motif and thus the nucleotide-binding mode seems to be conserved in all P-type ATPases, except the heavy metal-transporting (class IB) ATPases. Expand
Investigations on the Nucleotide Binding Domain of KdpB by NMR Spectroscopy and Solution Structure of an α4β7 Integrin Antagonist
The KdpFABC complex of E. coli, a P-type ATPase (class IA), is a high-affinity K+ uptake system that operates only when the cell experiences severe K+ limitation. The tertiary structure of theExpand
...
1
2
3
...

References

SHOWING 1-10 OF 39 REFERENCES
Structure and function of the Kdp-ATPase of Escherichia coli.
TLDR
The kdpFABC operon of Escherichia coli consists of the four structural genes kdpF, kdpA, KdpB, and kdpC and it was shown that the KdpF subunit remains associated with the purified complex. Expand
The KdpF Subunit Is Part of the K+-translocating Kdp Complex of Escherichia coli and Is Responsible for Stabilization of the Complex in Vitro *
TLDR
Upon expression of this operon in minicells, a so far unrecognized small hydrophobic polypeptide, KdpF, could be identified on high resolution SDS-polyacrylamide gels and proved to be indispensable for a functional enzyme complex in vitro. Expand
Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli.
TLDR
A structure in which KdpC could be one of the connecting links between the energy-delivering sub unit KdpB and the K+-transporting subunit KdpA is suggested by these data. Expand
The KDP ATPase of Escherichia coli.
TLDR
The role of K + as a preferred and essential osmoregulatory ion in bacteria explains the widespread distribution of the Kdp-type ATPase among distantly related eubacterial groups. Expand
The kdp system of Clostridium acetobutylicum: cloning, sequencing, and transcriptional regulation in response to potassium concentration
TLDR
The complete sequence of the kdp gene region of Clostridium acetobutylicum has been determined and Expression of the clostridial kdp genes, including the unique kdpX gene, was found to be inducible by low potassium concentrations. Expand
The KDP ATPase of Escherichia coli a
Potassium transport across the cytoplasmic membrane of Escherichia coli is a complex process involving multiple and separate systems for influx and efflux. (See reviews by Walderhaug et a1.l andExpand
The sensor kinase KdpD and the response regulator KdpE control expression of the kdpFABC operon in Escherichia coli.
TLDR
Kdp is the only K+-ATPase so far identified in bacteria; a P-type ATPase in Enterococcus hirae that was believed to take up K + now appears to transport Cu 2+ (Odermatt et al., 1993). Expand
Does the KdpA subunit from the high affinity K(+)-translocating P-type KDP-ATPase have a structure similar to that of K(+) channels?
Evidence is presented that the transmembrane KdpA subunit of the high affinity K(+)-translocating P-type Kdp-ATPase is evolutionarily derived from the superfamily of 2TM-type K(+) channels inExpand
Genetic Evidence for Two Sequentially Occupied K+ Binding Sites in the Kdp Transport ATPase (*)
TLDR
Substrate binding sites in Kdp, a P-type ATPase of Escherichia coli, were identified by the isolation and characterization of mutants with reduced affinity for K+, its cation substrate, suggesting that KdpA has 10 membrane-spanning segments and forms two separate and distinct sites where K+ is bound. Expand
Truncation of Amino Acids 12–128 Causes Deregulation of the Phosphatase Activity of the Sensor Kinase KdpD of Escherichia coli *
TLDR
The results suggest that amino acids 12–128 of KdpD are important for its activity and that an additional ATP-binding site in the N-terminal region seems to be involved in modulation of the phosphatase activity. Expand
...
1
2
3
4
...