btuD Antibody

1. The periplasmic soluble binding protein BtuF binds the vitamin B12 and the transmembrane and ATPase domains BtuCD mediate the translocation. PMID: 29162829
2. study used molecular dynamics simulations to investigate the atomic-level mechanism of conformational coupling in the ABC transporter BtuCD-F PMID: 27276259
3. ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations PMID: 27870912
4. Data suggest that the asymmetric crystal structure of BtuCD-F is an intermediate state in the process of reverse inward-facing to outward-facing (I-->O) transition. PMID: 22272354
5. Data suggest that BtuF does not discriminate between, or impose, asymmetric conformations of BtuC/BtuD complex. Data confirm conformational disorder observed in BtuC/BtuD/BtuF crystals. PMID: 22569249
6. Data provide insights into the subunit interactions of an ABC transporter and lays the foundation for studies of the reassembly of BtuCD. PMID: 21599645
7. 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 PMID: 17673622
8. ATP-binding cassette transporter BtuCD mediating vitamin B(12) uptake in Escherichia coli couples the energy of ATP hydrolysis to the translocation of vitamin B(12) across the membrane into the cell. PMID: 17951296

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KEGG: ecj:JW1699

STRING: 316385.ECDH10B_1845