Supplementary Materials

Supplementary Materials for:

Structural basis for the preference of the Arabidopsis thaliana phosphatase RLPH2 for tyrosine-phosphorylated substrates

Anne-Marie Labandera, R. Glen Uhrig, Keaton Colville, Greg B. Moorhead,* Kenneth K. S. Ng*

*Corresponding author. Email: moorhead{at} (G.B.M.); ngk{at} (K.K.S.N.)

This PDF file includes:

  • Fig. S1. Multiple sequence alignment of AtRLPH2 with other RLPH2 class members.
  • Fig. S2. Multiple sequence alignment of AtRLPH2 with other PPP family members from A. thaliana.
  • Fig. S3. Enzymatic activity of RLPH2 mutated in phosphothreonine-binding and gatekeeper residues.
  • Fig. S4. Different rotamers may be adopted by phosphothreonine in the pTEpY peptide substrate versus threonine in the TEpY peptide substrate.
  • Fig. S5. Location of motif 1 in RLPH2.
  • Table S1. Accession numbers of proteins used for sequence alignments.
  • Table S2. Primers used to create the AtRLPH2-V5-H6 mutants.
  • Legend for movie S1

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Other Supplementary Material for this manuscript includes the following:

  • Movie S1 (.mp4 format). AtRLPH2 substrate-binding groove.

© 2018 American Association for the Advancement of Science