Fig. 2: MX structure of PLproCoV-2 bound to human ISG15 and K48-Ub2 reveals differential usage of distal domains. | Nature Communications

Fig. 2: MX structure of PLproCoV-2 bound to human ISG15 and K48-Ub2 reveals differential usage of distal domains.

From: Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin

Fig. 2: MX structure of PLproCoV-2 bound to human ISG15 and K48-Ub2 reveals differential usage of distal domains.The alternative text for this image may have been generated using AI.

Schematic of PLpro bound to (a, left) hISG15 and (b, left) K48-linked Ub2. PLpro is shown in gray, with an active site indicated in yellow. hISG15 is shown in magenta. Proximal and distal Ubs are pink and white, respectively. Crystal structures of PLproCoV-2 bound to (a, right) hISG15 and (b, right) K48-Ub2. PLpro (C111S or C111S, D286N) is shown in cartoon representation, hISG15 and K48-Ub2 are shown as backbone traces. PLpro, hISG15, and K48-Ub2 are colored as in (a, left) and (b, left). c Overlay of crystal structures of bound hISG15 (magenta, PDB ID: 7RBS, this study) and unbound hISG15 (blue, PDB ID: 7S6P, this study). d Overlay of bound conformation of K48-linked Ub2 observed in complex with PLproCoV-1 (PDB ID: 5E6J) with unbound conformation of K48-linked Ub2 (PDB ID: 7S6O, this study). The proximal Ub of both bound and unbound conformations is shown in pink, the distal Ub of bound conformation is shown in white, and the distal Ub of unbound conformation is shown in blue. e Overlay of bound conformation of K48-linked Ub2 observed in complex with PLproCoV-1 (PDB ID: 5E6J) with unbound open conformation of Ub2 (PDB ID: 3NS8). Ub units are shown as in (d). f Overlay of bound conformation of K48-linked Ub2 observed in complex with PLproCoV-1 (PDB ID: 5E6J) with unbound closed conformation of Ub2 (PDB ID: 1AAR). Ub units are shown as in (d). The intramolecular Ub-Ub interface is indicated with an arrow. g Structural overlay of PLproCoV-2:hISG15 and PLproCoV-2:Ub2 (PDB ID: 7RBR, this study). Proteins are shown in cartoon and colored gray (PLpro), magenta (hISG15), and orange (Ub2). h Zoom in of the boxed area in (g) representing overlay of the proximal domain of hISG15 and Ub. The proximal domain of hISG15 and Ub are represented as in (g). Rotation of the binding surface is indicated with arrows. i, j Comparison of the binding surfaces of hISG15 (i) and Ub1 (j). The proximal domain of hISG15 and Ub are represented as in (g). Key residues are shown in space fill representation.

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