Ontology highlight
ABSTRACT:
SUBMITTER: Oldham ML
PROVIDER: S-EPMC3174604 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Oldham Michael L ML Chen Jue J
Proceedings of the National Academy of Sciences of the United States of America 20110808 37
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 specifi ...[more]