2qi9

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|PDB= 2qi9 |SIZE=350|CAPTION= <scene name='initialview01'>2qi9</scene>, resolution 2.600&Aring;
|PDB= 2qi9 |SIZE=350|CAPTION= <scene name='initialview01'>2qi9</scene>, resolution 2.600&Aring;
|SITE=
|SITE=
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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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|LIGAND= <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>
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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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|ACTIVITY= <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>
|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])
|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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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qi9 OCA], [http://www.ebi.ac.uk/pdbsum/2qi9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qi9 RCSB]</span>
}}
}}
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[[Category: Niederer, M.]]
[[Category: Niederer, M.]]
[[Category: Perozo, E.]]
[[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]]
 
[[Category: atp-binding]]
[[Category: atp-binding]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: transport]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:49:31 2008''

Revision as of 01:49, 31 March 2008

Image:2qi9.jpg


PDB ID 2qi9

Drag the structure with the mouse to rotate
, resolution 2.600Å
Ligands: , , , ,
Gene: btuC (Escherichia coli), btuD (Escherichia coli), btuF (Escherichia coli)
Activity: Vitamin B12-transporting ATPase, with EC number 3.6.3.33
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2QI9 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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