1l7v

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<StructureSection load='1l7v' size='340' side='right'caption='[[1l7v]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='1l7v' size='340' side='right'caption='[[1l7v]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1l7v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L7V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1L7V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1l7v]] is a 4 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=1L7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L7V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=V4O:CYCLO-TETRAMETAVANADATE'>V4O</scene></td></tr>
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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]] 3.2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=V4O:CYCLO-TETRAMETAVANADATE'>V4O</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BTUC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), BTUD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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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=1l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7v OCA], [https://pdbe.org/1l7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l7v RCSB], [https://www.ebi.ac.uk/pdbsum/1l7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l7v ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vitamin_B12-transporting_ATPase Vitamin B12-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.33 3.6.3.33] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7v OCA], [http://pdbe.org/1l7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l7v RCSB], [http://www.ebi.ac.uk/pdbsum/1l7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l7v ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BTUC_ECOLI BTUC_ECOLI]] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004] [[http://www.uniprot.org/uniprot/BTUD_ECOLI BTUD_ECOLI]] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system (By similarity).
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[https://www.uniprot.org/uniprot/BTUC_ECOLI BTUC_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1l7v 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=1l7v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The ABC transporters are ubiquitous membrane proteins that couple adenosine triphosphate (ATP) hydrolysis to the translocation of diverse substrates across cell membranes. Clinically relevant examples are associated with cystic fibrosis and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we report the crystal structure at 3.2 angstrom resolution of the Escherichia coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.
 
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The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism.,Locher KP, Lee AT, Rees DC Science. 2002 May 10;296(5570):1091-8. PMID:12004122<ref>PMID:12004122</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 1l7v" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[ABC transporter|ABC transporter]]
*[[ABC transporter|ABC transporter]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Vitamin B12-transporting ATPase]]
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[[Category: Lee AT]]
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[[Category: Lee, A T]]
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[[Category: Locher KP]]
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[[Category: Locher, K P]]
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[[Category: Rees DC]]
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[[Category: Rees, D C]]
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[[Category: Abc transporter]]
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[[Category: Atp binding cassette]]
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[[Category: Atp hydrolysis]]
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[[Category: Integral membrane protein]]
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[[Category: Transport protein-hydrolase complex]]
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[[Category: Vitamin b12]]
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Revision as of 08:07, 3 April 2024

Bacterial ABC Transporter Involved in B12 Uptake

PDB ID 1l7v

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