2qi9

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[[Image:2qi9.jpg|left|200px]]
 
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{{Structure
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==ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF==
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|PDB= 2qi9 |SIZE=350|CAPTION= <scene name='initialview01'>2qi9</scene>, resolution 2.600&Aring;
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<StructureSection load='2qi9' size='340' side='right'caption='[[2qi9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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<table><tr><td colspan='2'>[[2qi9]] is a 5 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=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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|ACTIVITY= [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]
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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]] 2.6&#8491;</td></tr>
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|GENE= btuC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), btuD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), btuF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<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=MSE:SELENOMETHIONINE'>MSE</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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}}
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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]
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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/initialview03.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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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 2qi9" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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 3D structures|ABC transporter 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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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__TOC__
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</StructureSection>
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==Reference==
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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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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Vitamin B12-transporting ATPase]]
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[[Category: Goetz BA]]
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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 RN]]
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[[Category: Hvorup, R N.]]
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[[Category: Locher KP]]
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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.]]
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[[Category: 1PE]]
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[[Category: PEG]]
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[[Category: PO4]]
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[[Category: SO4]]
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[[Category: atp-binding]]
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[[Category: hydrolase]]
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[[Category: inner membrane]]
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[[Category: membrane]]
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[[Category: membrane protein]]
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[[Category: nucleotide-binding]]
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[[Category: periplasm]]
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[[Category: transmembrane]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:06 2008''
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Current revision

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

PDB ID 2qi9

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