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ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF
Author(s) -
Locher Kaspar P,
Borths Elizabeth
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00289-3
Subject(s) - atp binding cassette transporter , transporter , lipid bilayer , atp hydrolysis , adenosine triphosphate , mechanism (biology) , chemistry , transport protein , biophysics , substrate (aquarium) , bilayer , membrane transport protein , biochemistry , microbiology and biotechnology , membrane , biology , enzyme , atpase , physics , gene , ecology , quantum mechanics
ABC transporters are ubiquitous membrane proteins that facilitate unidirectional substrate translocation across the lipid bilayer. Over the past five years, new crystal structures have advanced our understanding of how ABC transporters couple adenosine triphosphate (ATP) hydrolysis to substrate transport. In the following, we will briefly review the results of these structural investigations and outline their mechanistic implications.