Crystal stuctures of MglB‐2 (TP0684), a topologically variant d‐glucose‐binding protein from Treponema pallidum,reveal a ligand‐induced conformational change |
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Authors: | Chad A Brautigam Ranjit K Deka Wei Z Liu Michael V Norgard |
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Institution: | 1. Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas;2. Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas, Texas |
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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. |
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Keywords: | ABC transporter syphilis spirochete glucose‐binding protein conformational change |
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