Abstract
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.
Original language | English (US) |
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Pages (from-to) | 880-885 |
Number of pages | 6 |
Journal | Protein Science |
Volume | 27 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2018 |
Keywords
- ABC transporter
- conformational change
- glucose-binding protein
- spirochete
- syphilis
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology