Fig. 1: Nucleotide cleft water networks are remodelled upon phosphate release by F-actin.
From: Bending forces and nucleotide state jointly regulate F-actin structure
a, Cryo-EM maps of ADP–F-actin (left, shades of blue) and ADP-Pi–F-actin (right, shades of orange). ADP (green) and water (magenta) densities are shown. BE, barbed end; PE, pointed end. b, Atomic models of the ADP–F-actin (blue) and ADP-Pi–F-actin nucleotide (nuc.) clefts (orange) are shown in Cα representation. Top, carved transparent grey density is displayed for ADP (green), PO43− (yellow), Mg2+ (light green) and water molecules (violet). In ADP/PO43−, nitrogen atoms are blue, oxygen atoms are red and phosphorous atoms are yellow. Bottom, the backbone and side chain residues involved in putative hydrogen-bonding networks (dashed lines) are displayed and coloured by heteroatom. c, Superposition of individual ADP–F-actin (blue) and ADP-Pi–F-actin (orange) protomers, displayed in Cα representation.
