2qi9

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

spinqualitylabelsall models 2qi9, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qi9 is a 5 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, PEG, PO4, SO4 NonStd Res: MSE Gene: btuC ("Bacillus coli" Migula 1895), btuD ("Bacillus coli" Migula 1895), btuF ("Bacillus coli" Migula 1895) Activity: Vitamin B12-transporting ATPase, with EC number 3.6.3.33 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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] [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. [BTUD_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA