View source for 6bgd


==The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound ligand==
<StructureSection load='6bgd' size='340' side='right'caption='[[6bgd]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bgd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum_subsp._pallidum_str._Nichols Treponema pallidum subsp. pallidum str. Nichols]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BGD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgd OCA], [https://pdbe.org/6bgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bgd RCSB], [https://www.ebi.ac.uk/pdbsum/6bgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MGLB_TREPA MGLB_TREPA] May be involved in the transport of sugars. May have a role in chemotaxis.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:29318719</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bgd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema pallidum subsp. pallidum str. Nichols]]
[[Category: Brautigam CA]]
[[Category: Deka RK]]
[[Category: Norgard MV]]