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Crystal stuctures of MglB‐2 (TP0684), a topologically variant d ‐glucose‐binding protein from Treponema pallidum, reveal a ligand‐induced conformational change
Author(s) -
Brautigam Chad A.,
Deka Ranjit K.,
Liu Wei Z.,
Norgard Michael V.
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3373
Subject(s) - treponema , conformational change , chemistry , ligand (biochemistry) , crystal structure , crystallography , topology (electrical circuits) , biochemistry , biophysics , biology , syphilis , receptor , virology , mathematics , combinatorics , human immunodeficiency virus (hiv)
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 .