5sv0: Difference between revisions

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 <StructureSection load='5sv0' size='340' side='right'caption='[[5sv0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5sv0]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SV0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5sv0]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SV0 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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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]] 2.6&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5sv1|5sv1]]</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=5sv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sv0 OCA], [https://pdbe.org/5sv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sv0 RCSB], [https://www.ebi.ac.uk/pdbsum/5sv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sv0 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">exbB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1])</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=5sv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sv0 OCA], [http://pdbe.org/5sv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sv0 RCSB], [http://www.ebi.ac.uk/pdbsum/5sv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sv0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EXBB_ECO57 EXBB_ECO57]] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
+[https://www.uniprot.org/uniprot/EXBB_ECOLI EXBB_ECOLI] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the proton motive force at the inner membrane to transduce energy to the outer membrane via TonB. Here, we structurally characterize the Ton complex from Escherichia coli using X-ray crystallography, electron microscopy, double electron-electron resonance (DEER) spectroscopy, and crosslinking. Our results reveal a stoichiometry consisting of a pentamer of ExbB, a dimer of ExbD, and at least one TonB. Electrophysiology studies show that the Ton subcomplex forms pH-sensitive cation-selective channels and provide insight into the mechanism by which it may harness the proton motive force to produce energy.
-Structural insight into the role of the Ton complex in energy transduction.,Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R, Buchanan SK Nature. 2016 Sep 21. doi: 10.1038/nature19757. PMID:27654919<ref>PMID:27654919</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5sv0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[ExbB|ExbB]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ecod1]]
+[[Category: Escherichia coli DH1]]
 [[Category: Large Structures]]
-[[Category: Botos, I]]
+[[Category: Botos I]]
-[[Category: Buchanan, S K]]
+[[Category: Buchanan SK]]
-[[Category: Celia, H]]
+[[Category: Celia H]]
-[[Category: Lloubes, R]]
+[[Category: Lloubes R]]
-[[Category: Noinaj, N]]
+[[Category: Noinaj N]]
-[[Category: Channel]]
-[[Category: Exbb]]
-[[Category: Membrane protein]]
-[[Category: Pore]]
-[[Category: Transport protein]]