7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Thiobacillus denitrificans ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Escherichia coli ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus NBRC 13953 ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus JCM 1002 ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus NCIMB 11778 ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cobinamide-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446128 7.6.2.8 ATP + H2O + cyanocobalamin-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ADP + phosphate + cyanocobalamin[side 2] + [cobalamin-binding protein][side 1] - ? 446129 7.6.2.8 ATP + H2O + cyanocobalamin-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 Classical Ogawa 395 ADP + phosphate + cyanocobalamin[side 2] + [cobalamin-binding protein][side 1] - ? 446129 7.6.2.8 ATP + H2O + cyanocobalamin-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ATCC 39541 ADP + phosphate + cyanocobalamin[side 2] + [cobalamin-binding protein][side 1] - ? 446129 7.6.2.8 ATP + H2O + cyanocobalamin-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 O395 ADP + phosphate + cyanocobalamin[side 2] + [cobalamin-binding protein][side 1] - ? 446129 7.6.2.8 ATP + H2O + dicyanocobinamide-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ADP + phosphate + dicyanocobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446148 7.6.2.8 ATP + H2O + dicyanocobinamide-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 Classical Ogawa 395 ADP + phosphate + dicyanocobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446148 7.6.2.8 ATP + H2O + dicyanocobinamide-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ATCC 39541 ADP + phosphate + dicyanocobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446148 7.6.2.8 ATP + H2O + dicyanocobinamide-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 O395 ADP + phosphate + dicyanocobinamide[side 2] + [cobalamin-binding protein][side 1] - ? 446148 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Thiobacillus denitrificans ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Homo sapiens ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Escherichia coli ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus NBRC 13953 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus JCM 1002 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 Classical Ogawa 395 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus NCIMB 11778 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 ATCC 39541 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Vibrio cholerae serotype O1 O395 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] - Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] - ? 446185 7.6.2.8 ATP + H2O + vitamin B12/out - Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out - Haemophilus influenzae ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out - Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out - Mycobacterium tuberculosis ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out 480 ns multicopy molecular dynamics simulations performed, dynamics of apo and holo forms of the protein analyzed, opening and closing motions more pronounced in the apo form Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out crystal structure of BtuCD-F complex determined, BtuF protein shown to be bound to the periplasmic face of BtuCD Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out elastic normal mode analysis of BtuCD performed, mechanism of vitamin B12 transport cycle proposed Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out molecular dynamics on the vitamin B12-bound BtuF protein, energetics and mechanism of BtuF protein analyzed, opening and closing motions shown to be more pronounced in the apo form Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out nucleotide binding and release in the vitamin B12 importer BtuCD analyzed, perturbed elastic network calculations and biased molecular dynamics simulations applied, peristaltic forces suggested to exclude vitamin B12 from the transporter pore Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out simulation studies performed, analysis of principal components shown, with and without bound ATP Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 ATP + H2O + vitamin B12/out BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the periplasm into the cytoplasm of Escherichia coli. BtuD is complexed with BtuC, a permease protein, and BtuF, a periplasmic binding protein, structure, overview Escherichia coli ADP + phosphate + vitamin B12/in - ? 141441 7.6.2.8 additional information metal-chelate-type ABC transporter HI1470/1 is homologous with vitamin B12 importer BtuCD but exhibits a distinct inward-facing conformation in contrast to the outward-facing conformation of BtuCD. The outward-facing conformation of HI1470/1 is considered to be one of the intermediate states in the translocation cycle of BtuCD Haemophilus influenzae ? - ? 89 7.6.2.8 additional information BtuCD alone or the BtuCD-F complex do not bind vitamin B12. Only free, uncomplexed BtuF binds vitamin B12 with high affinity. Upon binding of BtuF to BtuCD, vitamin B12 is released from BtuF and is only transiently associated with the complex Escherichia coli ? - ? 89 7.6.2.8 additional information BtuCD forms a stable complex with the vitamin B12 binding protein BtuF. Using protein docking and MD simulation studies it is shown that holo-BtuF stabilizes the open conformation of BtuCD, whereas the transporter begins to close again when BtuF or vitamin B12 is removed suggesting BtuCD-F is capable of substrate sensitivity. BtuC transmembrane helices 3 and 5, the L-loops and the adjacent helices comprised of BtuC residues 170-180 are identified as hotspots of conformational change Escherichia coli ? - ? 89 7.6.2.8 additional information BtuCD forms an extremely stable complex with the vitamin B12 binding protein BtuF. Vitamin B12 accelerates complex dissociation rate, with ATP having an additional destabilizing effecf Escherichia coli ? - ? 89 7.6.2.8 additional information in the presence of vitamin B12, upon binding of ATP (or ATP analogues), no association between BtuF and BtuCD can be detected Escherichia coli ? - ? 89 7.6.2.8 additional information BtuM binds vitamin B12 in its base-off conformation, in which the 5,6-dimethylbenzimidazole moiety does not bind to the cobalt ion, but with a cysteine residue as axial ligand of the corrin cobalt ion, BtuMTd binds cobalamin (Cbl) using cysteine ligation. In contrast, at physiological pH the conformation of free Cbl in aqueous solution is base-on with the 5,6-dimethylbenzimidazole moiety coordinated to the cobalt ion in the alpha-axial position Thiobacillus denitrificans ? - ? 89 7.6.2.8 additional information VcBtuF, the periplasmic substrate binding protein (PBP) of putative ABC transporter BtuF-CD of Vibrio cholerae O395, binds cyanocobalamin and dicyanocobinamide with micromolar dissociation constants (Kd). Productive internalization of these nutrients Vibrio cholerae serotype O1 ? - ? 89 7.6.2.8 additional information a vitamin B12 molecule remains bound to the liposome-reconstituted transporter complex for tens of seconds, during which several ATP hydrolysis cycles can take place, before it is being transported across the membrane. Measurements of fluorescence changes on BtuCD induced by BtuF and ATP, transport of single vitamin B12 molecules, overview Escherichia coli ? - ? 89 7.6.2.8 additional information BtuCD-F catalyzes the uptake of cobinamide, a cobalamin precursor, and cobalamin. BtuCD-catalyzed in vitro transport of cyano-cobinamide and of cobalamin is ATP- and BtuF-dependent. Tryptophan residue W66 of BtuF is involved in the substrate binding of cobalamin Escherichia coli ? - ? 89 7.6.2.8 additional information BtuM binds vitamin B12 in its base-off conformation, in which the 5,6-dimethylbenzimidazole moiety does not bind to the cobalt ion, but with a cysteine residue as axial ligand of the corrin cobalt ion, BtuMTd binds cobalamin (Cbl) using cysteine ligation. In contrast, at physiological pH the conformation of free Cbl in aqueous solution is base-on with the 5,6-dimethylbenzimidazole moiety coordinated to the cobalt ion in the alpha-axial position. The membrane environment also appears to preclude Cbl binding to purified BtuMTd, as binding is observed only when the substrate is added before solubilisation. BtuMTd also catalyses cysteine-mediated decyanation of vitamin B12 Thiobacillus denitrificans ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus ? - ? 89 7.6.2.8 additional information the enzyme possesses equal levels of acyl-CoA thioesterase activity, ATPase and thioesterase activities of liposome-reconstituted human ABCD4, overview Homo sapiens ? - ? 89 7.6.2.8 additional information VcBtuF shows a distinctive phenomenon of heme binding with comparable affinity to vitamin B12 Vibrio cholerae serotype O1 ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus NBRC 13953 ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus JCM 1002 ? - ? 89 7.6.2.8 additional information VcBtuF, the periplasmic substrate binding protein (PBP) of putative ABC transporter BtuF-CD of Vibrio cholerae O395, binds cyanocobalamin and dicyanocobinamide with micromolar dissociation constants (Kd). Productive internalization of these nutrients Vibrio cholerae serotype O1 Classical Ogawa 395 ? - ? 89 7.6.2.8 additional information VcBtuF shows a distinctive phenomenon of heme binding with comparable affinity to vitamin B12 Vibrio cholerae serotype O1 Classical Ogawa 395 ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus NCIMB 11778 ? - ? 89 7.6.2.8 additional information VcBtuF, the periplasmic substrate binding protein (PBP) of putative ABC transporter BtuF-CD of Vibrio cholerae O395, binds cyanocobalamin and dicyanocobinamide with micromolar dissociation constants (Kd). Productive internalization of these nutrients Vibrio cholerae serotype O1 ATCC 39541 ? - ? 89 7.6.2.8 additional information VcBtuF shows a distinctive phenomenon of heme binding with comparable affinity to vitamin B12 Vibrio cholerae serotype O1 ATCC 39541 ? - ? 89 7.6.2.8 additional information VcBtuF, the periplasmic substrate binding protein (PBP) of putative ABC transporter BtuF-CD of Vibrio cholerae O395, binds cyanocobalamin and dicyanocobinamide with micromolar dissociation constants (Kd). Productive internalization of these nutrients Vibrio cholerae serotype O1 O395 ? - ? 89 7.6.2.8 additional information VcBtuF shows a distinctive phenomenon of heme binding with comparable affinity to vitamin B12 Vibrio cholerae serotype O1 O395 ? - ? 89 7.6.2.8 additional information hemin does not compete with cobalamin-uptake. Although promiscuous among cobalamin variants and cobalamin precursors, ECF-CbrT is a dedicated vitamin B12 transporter Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 ? - ? 89