Fig. 4: Structural comparison of PRT1ZZ and p62/SQSTM1 ZZ domain. | Nature Communications

Fig. 4: Structural comparison of PRT1ZZ and p62/SQSTM1 ZZ domain.

From: Structural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin

Fig. 4

a Electrostatic surface of PRT1 and p62/SQSTM1 ZZ domains (PDB IDs: PRT1 [8zg9], p62/SQSTM1 [5yp7]). A negatively charged region of PRT1ZZ (left) is enclosed by L3, while that of the p62/SQSTM1 ZZ domain (right) is exposed. b Close-up view of structural comparison. The α-NH3 group of both N-degrons (YKFG and R-BiP peptides) is recognized by two conserved Asp residues. The non-conserved key residues of the PRT1ZZ participate in the interaction with the hydrophobic bulky N-degron.

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