Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.

  title={Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.},
  author={John E. Walker and Matti Saraste and Michael J. Runswick and Nicholas J. Gay},
  journal={The EMBO Journal},
The alpha‐ and beta‐subunits of membrane‐bound ATP synthase complex bind ATP and ADP: beta contributes to catalytic sites, and alpha may be involved in regulation of ATP synthase activity. The sequences of beta‐subunits are highly conserved in Escherichia coli and bovine mitochondria. Also alpha and beta are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both alpha and beta and in other… 
A P‐loop‐like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity
It is proposed that PAPS reductases may have evolved from ATP sulfurylases; the evolution of the new enzymatic function appears to be accompanied by a switch of the strongest functional constraint from the PP‐motif to the putative sulfate‐binding motif.
Adenine recognition: A motif present in ATP‐, CoA‐, NAD‐, NADP‐, and FAD‐dependent proteins
The adenylate‐binding motif reported is present in “ancient proteins” common to all living organisms, suggesting that adenine‐containing ligands and the common motif for binding them were exploited very early in evolution.
Escherichia coli DNA Polymerase III τ- and γ-Subunit Conserved Residues Required for Activity In Vivo and In Vitro
Mutation of a highly conserved residue within a fourth motif, VIc, inactivated clamp-loading activity and reduced ATPase activity in vitro, but the mutant gene, on a multicopy plasmid, retained complementing activity in vivo and the mutant genes also supported apparently normal replication and growth as a haploid, chromosomal allele.
A family of closely related ATP‐binding subunits from prokaryotic and eukaryotic cells
A comparison of a family of closely related ATP‐binding proteins identified provides valuable insights into the function and evolution of the multicomponent systems with which they are associated.
Two distinct ATP‐binding domains are needed to promote protein export by Escherichia coli SecA ATPase
The results show that SecA contains two essential ATP‐binding domains, which were essential for SecA‐dependent translocation ATPase and in vitro protein translocation activities.
Effects of lysine-to-glycine mutations in the ATP-binding consensus sequences in the AddA and AddB subunits on the Bacillus subtilis AddAB enzyme activities
The results suggest that the lysine residue in motif I of subunit AddA of the AddAB enzyme is not essential for the binding of the nucleotide but has a role in ATP hydrolysis, which is required for the exonuclease and helicase activities of the enzyme.
One Intact ATP-binding Subunit Is Sufficient to Support ATP Hydrolysis and Translocation in an ABC Transporter, the Histidine Permease*
This work investigated the mechanism of action of such a dimer, both within the complex and in soluble form, by creating heterodimers between the wild type and mutant HisP proteins, and showed that the activating ability varies depending on the nature of the substitution of a well conserved residue, His-211.
Site-selected Mutagenesis of a Conserved Nucleotide Binding HXGH Motif Located in the ATP Sulfurylase Domain of Human Bifunctional 3′-Phosphoadenosine 5′-Phosphosulfate Synthase*
An important role for the HXGH histidines in the ATP sulfurylase activity of bifunctional PAPS synthase is suggested and the hypothesis that the highly conserved HX GH motif found in the oxidative phosphodiesterase domain of PAPS synthesis is involved in ATP binding and α-β phosphodiesters activity is supported.


EMBO fellowship and N.J.G. by an MRC studentship
  • 1982
  • Z. Physiol. Chem
  • 1982