Fig. 4: Redesigning xylanase and TEM β-lactamase.
From: Enhancing functional proteins through multimodal inverse folding with ABACUS-T
A Left: A structure of the natural xylanase (PDB ID: 4pn2) shown with the chemical formulas of the substrate and product (salmon sticks in the shown structures) of the enzymatic reaction; Right: The summary of experimental results of designed xylanase. The three sets of designed sequences were compared for the number of mutated residues, the number of designs with detectable activity at 35 °C, the number of designs with enhanced activity at 35 °C and the number of designs exhibiting above 50% residual activity after 60 °C heat treatment for 10 min (the denominators indicate the total numbers of experimentally characterized designs). B The same as A, but for designs of TEM β-lactamase (PDB ID: 1jvj) and changed experimental parameters as indicated. C Left: The relative activity at 35 °C of wild-type (normalized to 1.0) and redesigned xylanases with different methods. The bars and dots represent mean values and three independent biological replicates, and the error bars represent the standard deviations (SD).; Middle: The residual activity of wild-type xylanase and pxyl3-0.5 after heat treatment at 80 °C for a range of time from 0 min (normalized to 1.0) to 60 min. The dots represent mean values of three independent biological replicates, and the error bars represent SD; Right: The thermal melting curves of pxyl3-0.5 (colored in blue), txyl4 (colored in red), and native xylanase (colored in gray) according to CD signals at 222 nm. MRE: mean residue ellipticity. The values of Tm are indicated. D The same as (C) but Left: the relative activity at 37 °C of wild-type (normalized to 1.0) and redesigned lactamases with different methods; Middle: The residual activity of wild-type TEM β-lactamase, tlact2, plact2-0.2, plact2-0.5 after heat treatment at 50 °C for a range of time from 0 min (normalized to 1.0) to 60 min; Right: The thermal melting curves of wild-type TEM β-lactamase, tlact2, plact2-0.2, plact2-0.5 according to CD signals at 222 nm. Source data are provided as a Source Data file.
