Extended Data Fig. 1: Illustrations on the self-labeling property and structural analysis of HS protein.
From: Artificial metalloenzyme assembly in cellular compartments for enhanced catalysis
a, Mechanistic illustration of the self-labeling reactions of HaloTag–SNAPTag fusion protein. HaloTag is a modified haloalkane dehalogenase that can have its Asp106 residue irreversibly displace the chloride on a chloroalkyl substrate. SNAPTag is a truncated and modified human O6-alkylguanine-DNA alkyltransferase that can react with an O6-benzylguanine (BG) substrate with its Cys145 residue and displace the O6-benzylguaninyl moiety. The two coupling reactions are both bioorthogonal and efficient. b, Phase-separating region prediction made by ParSe v2 tool. The (EAAAK)4 linker sequence was predicted to be the major intrinsically disordered region (IDR) that promotes LLPS of the protein.
