2qvc
From Proteopedia
(Difference between revisions)
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==Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima== | ==Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima== | ||
| - | <StructureSection load='2qvc' size='340' side='right'caption='[[2qvc]]' scene=''> | + | <StructureSection load='2qvc' size='340' side='right'caption='[[2qvc]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVC FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVC FirstGlance]. <br> | ||
| - | </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=2qvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qvc OCA], [https://pdbe.org/2qvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qvc RCSB], [https://www.ebi.ac.uk/pdbsum/2qvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qvc ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2qvc TOPSAN]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2qvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qvc OCA], [https://pdbe.org/2qvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qvc RCSB], [https://www.ebi.ac.uk/pdbsum/2qvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qvc ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2qvc TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/2qvc_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/2qvc_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qvc ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qvc ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ABC transport systems have been characterized in organisms ranging from bacteria to humans. In most bacterial systems, the periplasmic component is the primary determinant of specificity of the transport complex as a whole. Here, the X-ray crystal structure of a periplasmic glucose-binding protein (GBP) from Thermotoga maritima determined at 2.4 A resolution is reported. The molecule consists of two similar alpha/beta domains connected by a three-stranded hinge region. In the current structure, a ligand (beta-D-glucose) is buried between the two domains, which have adopted a closed conformation. Details of the substrate-binding sites revealed features that determine substrate specificity. In toto, ten residues from both domains form eight hydrogen bonds to the bound sugar and four aromatic residues (two from each domain) stabilize the substrate through stacking interactions. | ||
| + | |||
| + | Structure of a periplasmic glucose-binding protein from Thermotoga maritima.,Palani K, Kumaran D, Burley SK, Swaminathan S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1460-4., doi: 10.1107/S1744309112045241. Epub 2012 Nov 19. PMID:23192024<ref>PMID:23192024</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2qvc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima
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