Locher KP 2004 ATP-binding cassette (ABC) transporters facilitate unidirectional translocation of chemically diverse substrates across cell or organelle membranes. The recently determined crystal structures of the vitamin B(12) importer BtuCD and its cognate binding protein BtuF have revealed critical architectural features that are probably shared by other ABC transporters. For example, the arrangement of the ABC domains and their interface with the membrane-spanning domains are probably conserved, whereas the number of transmembrane helices and their arrangement are not. Two distinct mechanistic schemes for how ABC engines couple ATP hydrolysis to substrate transport have been proposed recently and are being explored. https://sonar.ch/global/documents/47162 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2004.06.005 info:eu-repo/semantics/altIdentifier/pmid/15313236 Current opinion in structural biology. - 2004 ATP-Binding Cassette Transporters Escherichia coli Proteins Hydrolysis Models, Molecular Periplasmic Binding Proteins Protein Structure, Tertiary Protein Transport Structure-Activity Relationship Vitamin B 12 Structure and mechanism of ABC transporters. http://purl.org/coar/resource_type/c_6501