On allosteric modulation of P-type Cu(+)-ATPases.

@article{Mattle2013OnAM,
  title={On allosteric modulation of P-type Cu(+)-ATPases.},
  author={Daniel Mattle and Oleg Sitsel and Henriette Elisabeth Autzen and Gabriele Meloni and Pontus Emanuel Gourdon and Poul Nissen},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 13},
  pages={
          2299-308
        }
}
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Several novel P-type ATPase features are revealed, including a dual role in heavy-metal release, and as an internal counter ion, of an invariant, central histidine, in an archetypal PIB-4-ATPases.
Structure and ion-release mechanism of P IB-4-type ATPases 1 2
22 Transition metals, such as zinc, are essential micronutrients in all organisms, but 23 also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) 24 ATPases are crucial for…
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New methods of data partitioning and network visualization known as Transitivity Clustering and Protein Similarity Networks with existing biochemical data to examine properties such as length, speciation, and metal-binding motifs of the P1B-ATPase subfamily sequences reveal interesting relationships among the enzyme sequences of previously established subfamilies.
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Structural analysis indicates that Cu+ is bound at a high‐affinity transmembrane‐binding site in a trigonal‐planar coordination with the Cys residues of the conserved CPC motif of trans Membrane segment 4 (C382 and C384) and the Conserved Met residue of transmemBRane segment 6 (M717 of the MXXXS motif).
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The Cu(I)- and Zn(II)-ATPases are compared, scrutinizing the molecular differences that allow transport of these two distinct metal types, and possible future directions of research in the field are discussed.
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Learning algorithms engineered in a predictive machine is proposed to foresee the Q9LVV1 and O22180 substrate specificities (P-type ATPase like proteins) with 100 % prediction confidence and promising application of bioinformatics algorithms in classifying ATPases pumps is demonstrated.
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References

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TLDR
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TLDR
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