2qvc

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(New page: 200px<br /><applet load="2qvc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qvc, resolution 2.40&Aring;" /> '''Crystal structure of...)
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[[Image:2qvc.jpg|left|200px]]<br /><applet load="2qvc" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qvc, resolution 2.40&Aring;" />
 
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'''Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima'''<br />
 
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==About this Structure==
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==Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima==
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2QVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8] with <scene name='pdbligand=BGC:'>BGC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVC OCA].
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<StructureSection load='2qvc' size='340' side='right'caption='[[2qvc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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[[Category: Single protein]]
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== Structural highlights ==
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[[Category: Thermotoga maritima msb8]]
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<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>
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[[Category: Burley, S.K.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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[[Category: Kumaran, D.]]
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<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>
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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<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>
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[[Category: Palani, K.]]
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</table>
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[[Category: Swaminathan, S.]]
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== Evolutionary Conservation ==
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[[Category: BGC]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: 11013q]]
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Check<jmol>
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[[Category: abc sugar transporter]]
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<jmolCheckbox>
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[[Category: new york structural genomix research consortium]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/2qvc_consurf.spt"</scriptWhenChecked>
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[[Category: nysgxrc]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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[[Category: protein structure initiative ii]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: psi ii]]
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</jmolCheckbox>
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[[Category: structural genomics]]
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</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].
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[[Category: sugar-binding protein]]
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<div style="clear:both"></div>
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[[Category: transport protein]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:54:02 2008''
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2qvc" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Burley SK]]
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[[Category: Kumaran D]]
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[[Category: Palani K]]
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[[Category: Swaminathan S]]

Current revision

Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima

PDB ID 2qvc

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