Figure 5: Conformational plasticity of UCH-L5 is required for hydrolysing isopeptide bond of K48-linked di-ubiquitin. | Scientific Reports

Figure 5: Conformational plasticity of UCH-L5 is required for hydrolysing isopeptide bond of K48-linked di-ubiquitin.

From: Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome

Figure 5

(A) Orthogonal views of ubiquitin (purple) in complex with UCH-L5 (white) with the cross-over loop being partially disordered (dashed gold line). The location of the catalytic site is indicated by an inverted cyan triangle. (B) Model of K48-linked di-ubiquitin in complex with UCH-L5. The proximal ubiquitin is docked to the structure shown in (A) through manual rigid-body docking to avoid steric clashes. The cross-over loop is positioned at the interface between the distal and proximal ubiquitin molecules. (C) Schematic representation of the conformational rearrangement of the cross-over loop and adjacent structural elements in order to accommodate K48-linked di-ubiquitin.

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