Evolution of Substrate Specificities in the P-Type ATPase Superfamily

  title={Evolution of Substrate Specificities in the P-Type ATPase Superfamily},
  author={Kristian B. Axelsen and Michael Palmgren},
  journal={Journal of Molecular Evolution},
Abstract. P-type ATPases make up a large superfamily of ATP-driven pumps involved in the transmembrane transport of charged substrates. We have performed an analysis of conserved core sequences in 159 P-type ATPases. The various ATPases group together in five major branches according to substrate specificity, and not according to the evolutionary relationship of the parental species, indicating that invention of new substrate specificities is accompanied by abrupt changes in the rate of… 
P-type ATPases.
The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines.
The reproductive importance of P-type ATPases
At the Cutting Edge The reproductive importance of P-type ATPases
The dramatic change in the primary structure of one family member that may mediate transcription in the uterus is described, which is central to understanding the pump action of this family of enzymes.
Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review)
Generic features of P-type ATPases are compared with the rather unique KdpFABC complex of the enterobacterium Escherichia coli and a comprehensive overview of common principles of catalysis is given as well as of special aspects connected to distinct enzyme functions.
P‐Type ATPase Superfamily
The P‐type ATPase has become a protein superfamily and a comparative phylogenetic analysis demonstrates the relationship between the molecular evolution of these subfamilies and the establishment of the kingdoms of living things.
Prokaryotic Kdp-ATPase: Recent Insights into the Structure and Function of KdpB
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.
Type IV (P4) and V (P5) P-ATPases in Lipid Translocation and Membrane Trafficking
In this chapter, present knowledge concerning the role of P4- and P5-type pumps in lipid transport and membrane trafficking will be discussed.
P-type ATPases at a glance
P-type ATPases are a large family of integral membrane transporters that are of vital importance in all kingdoms of life. In eponymous distinction from the other main classes of transport ATPase –
Topogenic Motifs in P-type ATPases
  • K. Geering
  • Biology, Chemistry
    The Journal of Membrane Biology
  • 2000
It appears that P-typeA T P ases did not evolve at a constant rate and that acquisition of new ion specificity may have involvedrupt changes in the rate of sequence adaptations (Ax-elsen & Palmgren, 1998).


A Subfamily of P-Type ATPases with Aminophospholipid Transporting Activity
Studies in Saccharomyces cerevisiae suggest that aminophospholipid translocation is a general function of members of this family, and this work has cloned and sequenced the bovine enzyme.
Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum.
We have determined the DNA sequences of the genes encoding the three structural proteins of the Kdp-ATPase, an ATP-driven potassium transport system of Escherichia coli. Regions of the predicted
Changing the Ion Binding Specificity of the Escherichia coli H-transporting ATP Synthase by Directed Mutagenesis of Subunit c(*)
It is suggested that a X-glu-Ser-Y or X-Glu-Thr-Y sequence may provide a general structural motif for monovalent cation binding, and that the flexibility provided by residues X and Y will prove crucial to this structure.
Molecular Cloning of an Intracellular P-type ATPase from Dictyostelium That Is Up-regulated in Calcium-adapted Cells (*)
The cloned and sequenced cDNAs that encode a putative P-type Ca ATPase designated patA suggest that in Dictyostelium this organelle might function in Ca homeostasis as well as in water regulation.
Genetic Evidence for Two Sequentially Occupied K+ Binding Sites in the Kdp Transport ATPase (*)
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.
Gene fusion during the evolution of the tryptophan operon in Enterobacteriaceae
Analysis of one example of a possible gene fusion in tryptophan biosynthesis and an attempt to deduce the sequence of events responsible.
A Single Gene May Encode Differentially Localized Ca2+-ATPases in Tomato.
Data suggest that a single gene (LCA) may encode two P-type Ca2+-ATPase isoforms that are differentially localized in the tonoplast and plasma membrane of tomato roots.
Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes.
It is concluded that the Mg2+ ATPase is sufficient for the biochemical expression of the aminophospholipid translocase activity, which is responsible for the inward transport of phosphatidylserine andosphatidylethanolamine within the erythrocyte membrane.