論文 - 詳細
| RRC ID | 35566 |
|---|---|
| 著者 | Bao H, Duong F. |
| タイトル | ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter. |
| ジャーナル | J Biol Chem |
| Abstract |
The maltose transporter MalFGK(2) is a study prototype for ABC importers. During catalysis, the MalFG membrane domain alternates between inward and outward facing conformations when the MalK dimer closes and hydrolyzes ATP. Because a rapid ATP hydrolysis depends on MalE and maltose, it has been proposed that closed liganded MalE facilitates the transition to the outward facing conformation. Here we find that, in contrast to the expected, ATP is sufficient for the closure of MalK and for the conversion of MalFG to the outward facing state. The outward facing transporter binds MalE with nanomolar affinity, yet neither MalE nor maltose is necessary or facilitates the transition. Thus, the rapid hydrolysis of ATP observed in the presence of MalE and maltose is not because closed liganded MalE accelerates the formation of the outward facing conformation. These findings have fundamental implications for the description of the transport reaction. |
| 巻・号 | 288(5) |
| ページ | 3439-48 |
| 公開日 | 2013-2-1 |
| DOI | 10.1074/jbc.M112.431932 |
| PII | S0021-9258(20)46457-9 |
| PMID | 23243313 |
| PMC | PMC3561562 |
| MeSH | ATP-Binding Cassette Transporters / chemistry* ATP-Binding Cassette Transporters / metabolism* Adenosine Triphosphatases / metabolism Adenosine Triphosphate / pharmacology* Biological Transport / drug effects Escherichia coli Proteins / chemistry* Escherichia coli Proteins / metabolism* Fluorescence Kinetics Maltose / metabolism* Periplasmic Binding Proteins / metabolism Protein Binding / drug effects Protein Conformation Proteolipids / metabolism Titrimetry |
| IF | 4.238 |
| 引用数 | 19 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 各媒体での言及数の合計 | 0 |
| リソース情報 | |
| 原核生物(大腸菌) | BL21(DE3)? |