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

• Published in: Protein science Vol. 27; no. 4; pp. 880 - 885
• Main Authors: Brautigam, Chad A., Deka, Ranjit K., Liu, Wei Z., Norgard, Michael V.
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.04.2018; John Wiley and Sons Inc
• Subjects: ABC transporter; Bacterial infections; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; conformational change; Crystal structure; Crystallography, X-Ray; Glucose; Glucose - metabolism; glucose‐binding protein; Models, Molecular; Monosaccharide Transport Proteins - chemistry; Monosaccharide Transport Proteins - metabolism; Protein Conformation; Protein Structure Report; Protein Structure Reports; Proteins; Sexually transmitted diseases; spirochete; Spirochetes; STD; Syphilis; Topology; Treponema pallidum; Treponema pallidum - chemistry; syphilis; conformational change; glucose-binding protein; spirochete; ABC transporter
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1002/pro.3373

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. PDB Code(s): 6BGC; 6BGD