2gsk
From Proteopedia
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| - | {{STRUCTURE_2gsk| PDB=2gsk | SCENE= }} | ||
| - | ===Structure of the BtuB:TonB Complex=== | ||
| - | {{ABSTRACT_PUBMED_16741124}} | ||
| - | == | + | ==Structure of the BtuB:TonB Complex== |
| - | [[2gsk]] is a 2 chain structure with sequence from [ | + | <StructureSection load='2gsk' size='340' side='right'caption='[[2gsk]], [[Resolution|resolution]] 2.10Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2gsk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GSK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=CNC:CO-CYANOCOBALAMIN'>CNC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</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=2gsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsk OCA], [https://pdbe.org/2gsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gsk RCSB], [https://www.ebi.ac.uk/pdbsum/2gsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gsk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BTUB_ECOLI BTUB_ECOLI] Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins.[HAMAP-Rule:MF_01531] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/2gsk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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=2gsk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport. | ||
| + | |||
| + | Outer membrane active transport: structure of the BtuB:TonB complex.,Shultis DD, Purdy MD, Banchs CN, Wiener MC Science. 2006 Jun 2;312(5778):1396-9. PMID:16741124<ref>PMID:16741124</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2gsk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[BtuB|BtuB]] | + | *[[BtuB 3D structures|BtuB 3D structures]] |
*[[TonB|TonB]] | *[[TonB|TonB]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Banchs CN]] |
| - | [[Category: | + | [[Category: Purdy MP]] |
| - | [[Category: | + | [[Category: Shultis DD]] |
| - | [[Category: | + | [[Category: Wiener MC]] |
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Current revision
Structure of the BtuB:TonB Complex
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