6BGD
The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound ligand
Summary for 6BGD
| Entry DOI | 10.2210/pdb6bgd/pdb |
| Descriptor | Glucose/galactose-binding lipoprotein, 1,2-ETHANEDIOL, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | glucose, syphilis, sugar binding protein |
| Biological source | Treponema pallidum (strain Nichols) |
| Total number of polymer chains | 1 |
| Total formula weight | 40965.65 |
| Authors | Brautigam, C.A.,Norgard, M.V.,Deka, R.K. (deposition date: 2017-10-27, release date: 2018-01-31, Last modification date: 2023-10-25) |
| Primary citation | Brautigam, C.A.,Deka, R.K.,Liu, W.Z.,Norgard, M.V. Crystal structures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change. Protein Sci., 27:880-885, 2018 Cited by PubMed 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. PubMed: 29318719DOI: 10.1002/pro.3373 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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