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Phosphorylation Alters the Interaction of the Arabidopsis Phosphotransfer Protein AHP1 with Its Sensor Kinase ETR1

Figure 5

Electrostatic surface potential of the histidine phospho-transfer protein AHP1.

A structural model of AHP1 was built using MODELLER [44] interfaced by EASYMODELLER [45] with default options using the 3D structure of the histidine-containing phosphotransfer protein OsHP1, from rice (PDB code 1YVI). In this method the 3D-structure is generated in such a way that a set of spatial and empirically determined restraints are optimally satisfied. Electrostatic potentials for this model were calculated using PDB2PQR [46] and APBS [47]. Images were generated with PyMOL [48]. Solvent-accessible surface is colored according to the electrostatic potential [−5 kT/e red, +5 kT/e blue]. (A) and (C) side view, (B) and (D) top view. Catalytic residue H79 and residues defining the negative (residues D40-D65) and positive electrostatic surface potential (residues R114-K135) are labelled.

Figure 5

doi: https://doi.org/10.1371/journal.pone.0024173.g005