Structure and mechanism of ABC transporters.
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.
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland. locher@mol.biol.ethz.ch
Kaspar P
KP
Locher
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D033902:Periplasmic Binding Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology; D013329:Structure-Activity Relationship; D014805:Vitamin B 12 / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; C050021:BtuC peptide, E coli; C050022:BtuD peptide, E coli; D029968:Escherichia coli Proteins; D033902:Periplasmic Binding Proteins; C446048:btuF protein, E coli; D014805:Vitamin B 12