6bgd

The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound ligand

spinqualitylabelsall models 6bgd, resolution 1.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bgd is a 1 chain structure with sequence from Treponema pallidum subsp. pallidum str. Nichols. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.47Å Ligands: CA, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MGLB_TREPA May be involved in the transport of sugars. May have a role in chemotaxis. Publication Abstract from PubMed 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. This article is protected by copyright. All rights reserved. Crystal structures of MglB-2 (TP0684), a topologically variant D-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change.,Brautigam CA, Deka RK, Liu WZ, Norgard MV Protein Sci. 2018 Jan 10. doi: 10.1002/pro.3373. PMID:29318719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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