1L7V
Bacterial ABC Transporter Involved in B12 Uptake
Summary for 1L7V
| Entry DOI | 10.2210/pdb1l7v/pdb |
| Descriptor | VITAMIN B12 TRANSPORT SYSTEM PERMEASE PROTEIN BTUC, Vitamin B12 transport ATP-binding protein btuD, CYCLO-TETRAMETAVANADATE (3 entities in total) |
| Functional Keywords | abc transporter, integral membrane protein, atp binding cassette, atp hydrolysis, vitamin b12, transport protein-hydrolase complex, transport protein/hydrolase |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P06609 Cell inner membrane; Peripheral membrane protein: P06611 |
| Total number of polymer chains | 4 |
| Total formula weight | 126839.87 |
| Authors | Locher, K.P.,Lee, A.T.,Rees, D.C. (deposition date: 2002-03-18, release date: 2002-05-15, Last modification date: 2024-11-20) |
| Primary citation | Locher, K.P.,Lee, A.T.,Rees, D.C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science, 296:1091-1098, 2002 Cited by PubMed Abstract: 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. PubMed: 12004122DOI: 10.1126/science.1071142 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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