Conservation analysis and structure prediction
of the protein serine/threonine phosphatases:
Sequence similarity with diadenosine tetra-phosphatase
from Escherichia coli suggests homology to the
protein phosphatases

Geoffrey J. Barton, Patricia T. W. Cohen and David Barford

Laboratory of Molecular Biophysics
University of Oxford
Rex Richards Building
South Parks Road
Oxford OX1 3QU, U.K.

Medical Research Council Protein Phosphorylation Unit
Department of Biochemistry
University of Dundee
Dundee DD1 4HN, Scotland, U.K.

W. M. Keck Structural Biology Laboratory
Cold Spring Harbor Laboratory
Cold Spring Harbor
P.O. Box 100
N.Y. 11724, U.S.A.
Subdivision: Protein Chemistry and Structure
Corresponding author: Dr. G. J. Barton
Tel: (+44) 865 275368
Fax: (+44) 865 510454
e-mail: geoff@biop.ox.ac.uk

• Contents
• Summary
• Abbreviations
• Introduction
• Methods
  • Source of Sequences and Multiple Alignment
  • Conservation Analysis and Secondary Structure Prediction
• Results
  • Clustering of sequences
  • Similarity to Bacteriophage Protein Phosphatases and E. coli Tetra-Phosphatase
  • Invariant residues, secondary structure and insertions/deletions
    • Loop Predictions
    • Helix Predictions
    • Beta Strand Predictions
    • Ambiguous Predictions
• Discussion
  • Invariant Residues Suggest a Common Catalytic Mechanism
  • Change in charge sign
  • Phosphate binding site
  • Phosphoryl-Enyzme Intermediate
  • Are metal ions present at the catalytic centre?
  • Secondary Structure Prediction and Domain Structure
• Acknowledgements
• Figure Legends
  • Legend to Figure 1
  • Legend to Figure 2
• Tables
  • Table 1
  • Table 2
  • Table 3 - Changes in sign of potential charge
• References
• About this document ...