1l7v | pdb_00001l7v

Bacterial ABC Transporter Involved in B12 Uptake

spinqualitylabelsall models 1l7v, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1l7v is a 4 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: V4O NonStd Res: MSE Gene: BTUC ("Bacillus coli" Migula 1895), BTUD ("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] [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 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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