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[[Image:2gsk.gif|left|200px]]


{{Structure
==Structure of the BtuB:TonB Complex==
|PDB= 2gsk |SIZE=350|CAPTION= <scene name='initialview01'>2gsk</scene>, resolution 2.10&Aring;
<StructureSection load='2gsk' size='340' side='right'caption='[[2gsk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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>
<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>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE= btuB, bfe, cer, dcrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), tonB, exbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsk OCA], [http://www.ebi.ac.uk/pdbsum/2gsk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gsk RCSB]</span>
== 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/initialview03.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.


'''Structure of the BtuB:TonB Complex'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gsk" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[BtuB 3D structures|BtuB 3D structures]]
 
*[[TonB|TonB]]
==About this Structure==
== References ==
2GSK is a [[Protein complex]] structure of sequences from [http://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].
<references/>
 
__TOC__
==Reference==
</StructureSection>
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:[http://www.ncbi.nlm.nih.gov/pubmed/16741124 16741124]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Banchs, C N.]]
[[Category: Banchs CN]]
[[Category: Purdy, M P.]]
[[Category: Purdy MP]]
[[Category: Shultis, D D.]]
[[Category: Shultis DD]]
[[Category: Wiener, M C.]]
[[Category: Wiener MC]]
[[Category: beta-barrel]]
[[Category: membrane protein]]
[[Category: outer-membrane active transport]]
[[Category: tonb]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:20:56 2008''

Latest revision as of 08:08, 13 August 2026

Structure of the BtuB:TonB Complex

2gsk, resolution 2.10Å

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