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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: Nat Struct Mol Biol. 2014 Nov 2;21(12):1075–1081. doi: 10.1038/nsmb.2907

Figure 2. Different interaction modes between coronin and actin in ADP and ADP-BeFx states.

Figure 2

(a–d) Pseudo-atomic models obtained by fitting an atomic model of actin and our homology model of coronin into our cryoEM densities (see text). (a and b) Differences in the overall binding modes between coronin and actin in ADP (a) and ADP-BeFx (b) states. Actin is shown in ribbons colored by rainbow colors (N-terminal: blue, C-terminal: red), with each subunit delineated with its grey transparent surface that is derived from its atomic model; coronin is shown in gold ribbons. Key interacting amino acids between coronin and actin i+1 are shown in sticks and are highlighted in insets. (c and d) Different environments of Cys374 in ADP (c) and ADP-BeFx (d) states. Actin’s C-terminal loop 371–375 is in red; the C-terminus marked by “COOH”. (e) Fluorescence emission spectra of actin labeled with acrylodan at residue 374 in the ADP-actin-coronin complex and (f) the ADP-BeFx-actin-coronin complex. In panels (a–d), key residues are marked with labels of their single letter codes and residue numbers and are colored in black and purple for actin and coronin, respectively.