1PIX
Crystal structure of the carboxyltransferase subunit of the bacterial ion pump glutaconyl-coenzyme A decarboxylase
1PIX の概要
| エントリーDOI | 10.2210/pdb1pix/pdb |
| 分子名称 | Glutaconyl-CoA decarboxylase A subunit, SULFATE ION, FORMIC ACID, ... (4 entities in total) |
| 機能のキーワード | decarboxylase, biotin-dependent ion pump, carboxyltransferase, lyase |
| 由来する生物種 | Acidaminococcus fermentans |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 129511.43 |
| 構造登録者 | Wendt, K.S.,Schall, I.,Huber, R.,Buckel, W.,Jacob, U. (登録日: 2003-05-30, 公開日: 2003-08-05, 最終更新日: 2024-02-14) |
| 主引用文献 | Wendt, K.S.,Schall, I.,Huber, R.,Buckel, W.,Jacob, U. Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase Embo J., 22:3493-3502, 2003 Cited by PubMed Abstract: Glutaconyl-CoA decarboxylase is a biotin-dependent ion pump whereby the free energy of the glutaconyl-CoA decarboxylation to crotonyl-CoA drives the electrogenic transport of sodium ions from the cytoplasm into the periplasm. Here we present the crystal structure of the decarboxylase subunit (Gcdalpha) from Acidaminococcus fermentans and its complex with glutaconyl-CoA. The active sites of the dimeric Gcdalpha lie at the two interfaces between the mono mers, whereas the N-terminal domain provides the glutaconyl-CoA-binding site and the C-terminal domain binds the biotinyllysine moiety. The Gcdalpha catalyses the transfer of carbon dioxide from glutaconyl-CoA to a biotin carrier (Gcdgamma) that subsequently is decarboxylated by the carboxybiotin decarboxylation site within the actual Na(+) pump (Gcdbeta). The analysis of the active site lead to a novel mechanism for the biotin-dependent carboxy transfer whereby biotin acts as general acid. Furthermore, we propose a holoenzyme assembly in which the water-filled central channel of the Gcdalpha dimer lies co-axial with the ion channel (Gcdbeta). The central channel is blocked by arginines against passage of sodium ions which might enter the central channel through two side channels. PubMed: 12853465DOI: 10.1093/emboj/cdg358 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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