6bgd
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | The | + | ==The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound glucose== |
+ | <StructureSection load='6bgd' size='340' side='right' caption='[[6bgd]], [[Resolution|resolution]] 1.47Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6bgd]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGD FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgd OCA], [http://pdbe.org/6bgd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgd RCSB], [http://www.ebi.ac.uk/pdbsum/6bgd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgd ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Norgard, M | + | <div class="pdbe-citations 6bgd" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Brautigam, C A]] | ||
+ | [[Category: Deka, R K]] | ||
+ | [[Category: Norgard, M V]] | ||
+ | [[Category: Glucose]] | ||
+ | [[Category: Sugar binding protein]] | ||
+ | [[Category: Syphili]] |
Revision as of 05:57, 31 January 2018
The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound glucose
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