Figure 1: Characterization of the conformational dynamics of apo-SENP1 (C603S). | Nature Communications

Figure 1: Characterization of the conformational dynamics of apo-SENP1 (C603S).

From: Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding

Figure 1

(a) The closed catalytic channel of SENP1. SENP1 is shown as surface representation and the closed catalytic channel in apo-SENP1 (pdbid: 2IYC) is indicated with a circle (left panel). SUMO1 is shown in ribbon diagram (middle and right panels, pdbid:2IY1). A zoom-in view of the catalytic channel (right panel) is shown with side chains that are labelled with their residue numbers and coloured according to the timescale of their conformational dynamics. Red, microsecond dynamics detected by HzNz R1ρ only; green, micro–millisecond dynamics detected by CPMG only; and black, pico–millisecond dynamics detected by 1H–15N NOE, HzNz R1ρ and CPMG. (b) Representative broadened backbone NH resonances of residues Trp465, Trp534 and Leu466 that are at or near the catalytic channel from the 1H–15N HSQC spectrum of apo-SENP1. (c) Representative CPMG-relaxation dispersion profiles for the resonances of residues at the catalytic channel, measured by 600 (circle) and 700 (square) MHz NMR instruments. The error bars were obtained from duplicated measurements (see Methods section).

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