Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brautigam CA, Deka RK, Liu WZ, Norgard MV. Crystal structures of MglB-2 (TP0684), a topologically variant D-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change. Protein Sci. 2018 Jan 10. doi: 10.1002/pro.3373. PMID:29318719 doi:http://dx.doi.org/10.1002/pro.3373
