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2qi9

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[[Image:2qi9.jpg|left|200px]]
 
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==ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF==
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The line below this paragraph, containing "STRUCTURE_2qi9", creates the "Structure Box" on the page.
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<StructureSection load='2qi9' size='340' side='right'caption='[[2qi9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qi9]] is a 5 chain structure with sequence from [https://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=2QI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QI9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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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{{STRUCTURE_2qi9| PDB=2qi9 | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">btuC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), btuD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), btuF ([https://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Vitamin_B12-transporting_ATPase Vitamin B12-transporting ATPase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2qi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qi9 OCA], [https://pdbe.org/2qi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qi9 RCSB], [https://www.ebi.ac.uk/pdbsum/2qi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qi9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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] [[https://www.uniprot.org/uniprot/BTUF_ECOLI BTUF_ECOLI]] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.<ref>PMID:11790740</ref> [[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/2qi9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2qi9 ConSurf].
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<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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BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF. The lobes of BtuF are spread apart, and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F that was observed in the crystal structure. A comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a posttranslocation intermediate.
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'''ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF'''
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Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF.,Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, Locher KP Science. 2007 Sep 7;317(5843):1387-90. Epub 2007 Aug 2. PMID:17673622<ref>PMID:17673622</ref>
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==Overview==
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BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF. The lobes of BtuF are spread apart, and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F that was observed in the crystal structure. A comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a posttranslocation intermediate.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2QI9 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=2QI9 OCA].
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</div>
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<div class="pdbe-citations 2qi9" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF., Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, Locher KP, Science. 2007 Sep 7;317(5843):1387-90. Epub 2007 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17673622 17673622]
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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[[Category: Escherichia coli]]
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== References ==
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[[Category: Protein complex]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Large Structures]]
[[Category: Vitamin B12-transporting ATPase]]
[[Category: Vitamin B12-transporting ATPase]]
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[[Category: Goetz, B A.]]
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[[Category: Goetz, B A]]
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[[Category: Hollenstein, K.]]
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[[Category: Hollenstein, K]]
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[[Category: Hvorup, R N.]]
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[[Category: Hvorup, R N]]
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[[Category: Locher, K P.]]
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[[Category: Locher, K P]]
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[[Category: Niederer, M.]]
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[[Category: Niederer, M]]
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[[Category: Perozo, E.]]
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[[Category: Perozo, E]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:00:37 2008''
 

Current revision

ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF

PDB ID 2qi9

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