title: Snapshots of the maltose transporter during ATP hydrolysis.
abstract: ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(β,γ-imido)triphosphate or ADP in conjunction with phosphate analogs BeF(3)(-), VO(4)(3-), or AIF(4)(-), were determined to 2.2- to 2.4-Å resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.
authors.affiliation: Department of Biological Sciences, Purdue University, Howard Hughes Medical Institute, 240 Martin Jischke Boulevard, West Lafayette, IN 47907, USA.
authors.forename: Michael L
authors.initials: ML
authors.lastname: Oldham
authors.forename: Jue
authors.initials: J
authors.lastname: Chen
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D055162:Biocatalysis; D020134:Catalytic Domain; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008320:Maltose / Q000378:metabolism*; D058619:Maltose-Binding Proteins / Q000378:metabolism; D008958:Models, Molecular; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D050505:Mutant Proteins; D000266:Adenylyl Imidodiphosphate; D008320:Maltose; D000255:Adenosine Triphosphate