Fig. 3: E. coli LplA achieves higher-order assembly and phase separation through specific interfaces, which are dominated by electrostatic and hydrophobic interactions as revealed by mutation study of different amino acid residues. | Nature Communications

Fig. 3: E. coli LplA achieves higher-order assembly and phase separation through specific interfaces, which are dominated by electrostatic and hydrophobic interactions as revealed by mutation study of different amino acid residues.

From: A globular protein exhibits rare phase behavior and forms chemically regulated orthogonal condensates in cells

Fig. 3

a The asymmetric unit of the LplA crystal (PDB ID: 1X2G) consists of three LplA molecules (MolA, MolB and MolC). b–i The phase behavior of LplA in E. coli with various single-site mutations. Scale bars, 2 μm. Images are representative of three biological replicates. j Interaction interfaces involved in LplA self-assembly. The contact interface in the crystal structure 1X2G (distance <4 Å) is marked in magenta (left). The mutation sites that lead to complete disruption and weakening of LplA condensation are marked respectively in red and orange (right), the same marking color in Supplementary Table 3, 4. k A diagram illustrating the structural oligomerization of LplA through two types of interface interactions, which is the molecular basis for its phase behavior.

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