6bgc: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry~~ 6bgc is ~~ON HOLD until Paper~~ Publication

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

== Structural highlights ==

<table><tr><td colspan='2'>[[6bgc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGC FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <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=6bgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgc OCA], [http://pdbe.org/6bgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgc RCSB], [http://www.ebi.ac.uk/pdbsum/6bgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgc 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.

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Brautigam, C A]]

[[Category: Deka, R K]]

[[Category: Norgard, M V]]

[[Category: Glucose]]

[[Category: Sugar binding protein]]

[[Category: Syphili]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6bgc is ON HOLD  until Paper Publication
+==The crystal structure of the W145A variant of TpMglB-2 (Tp0684) with bound glucose==
+<StructureSection load='6bgc' size='340' side='right' caption='[[6bgc]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6bgc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BGC FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <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=6bgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bgc OCA], [http://pdbe.org/6bgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bgc RCSB], [http://www.ebi.ac.uk/pdbsum/6bgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bgc 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6bgc" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Brautigam, C A]]
+[[Category: Deka, R K]]
+[[Category: Norgard, M V]]
+[[Category: Glucose]]
+[[Category: Sugar binding protein]]
+[[Category: Syphili]]