Coupled Mutations-Enabled Glycerol Transportation in an Aquaporin Z Mutant.

ABSTRACT: Aquaporins are transmembrane channel proteins with key function being transportation of water or other small substrates. Escherichia coli Aqp Z transports water molecules only, whereas Glp F is permeable to glycerol. It is intriguing to explore the possibility to induce glycerol permeability in Aqp Z by targeted mutations. The Aqp Z mutants with mutated selectivity filter (SF) residues exhibit poor permeability for both glycerol and water. For addressing the complexity of protein systems, pair correlation information in protein sequence analyses is instructive to identify residues that are coupled by coevolution and motion. In this study, we analyze the correlation between residues and unravel the clustering patterns of coupled residues, beyond SF residues, in aquaglyceroporins (AQG

SUBMITTER: Ping Z 

PROVIDER: S-EPMC6641515 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature