Crystal stuctures of MglB‐2 (TP0684) a topologically variant d‐glucose‐binding protein from Treponema pallidum reveal a ligand‐induced conformational change

摘要

Previously, we determined the crystal structure of apo‐TpMglB‐2, a d‐glucose‐binding component of a putative ABC transporter from the syphilis spirochete Treponema pallidum. The protein had an unusual topology for this class of proteins, raising the question of whether the d‐glucose‐binding mode would be different in TpMglB‐2. Here, we present the crystal structures of a variant of TpMglB‐2 with and without d‐glucose bound. The structures demonstrate that, despite its aberrant topology, the protein undergoes conformational changes and binds d‐glucose similarly to other Mgl‐type proteins, likely facilitating d‐glucose uptake in T. pallidum.