5LS7
Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ
5LS7 の概要
| エントリーDOI | 10.2210/pdb5ls7/pdb |
| 分子名称 | Aspartate 1-decarboxylase, methyl radical, PanD maturation factor, ... (11 entities in total) |
| 機能のキーワード | protein derived cofactor, coenzyme a biosynthesis, protein complex, metabolic pathway regulation, lyase |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| 細胞内の位置 | Cytoplasm : P0A790 P0A790 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 33047.23 |
| 構造登録者 | |
| 主引用文献 | Arnott, Z.L.P.,Nozaki, S.,Monteiro, D.C.F.,Morgan, H.E.,Pearson, A.R.,Niki, H.,Webb, M.E. The Mechanism of Regulation of Pantothenate Biosynthesis by the PanD-PanZAcCoA Complex Reveals an Additional Mode of Action for the Antimetabolite N-Pentyl Pantothenamide (N5-Pan). Biochemistry, 56:4931-4939, 2017 Cited by PubMed Abstract: The antimetabolite pentyl pantothenamide has broad spectrum antibiotic activity but exhibits enhanced activity against Escherichia coli. The PanDZ complex has been proposed to regulate the pantothenate biosynthetic pathway in E. coli by limiting the supply of β-alanine in response to coenzyme A concentration. We show that formation of such a complex between activated aspartate decarboxylase (PanD) and PanZ leads to sequestration of the pyruvoyl cofactor as a ketone hydrate and demonstrate that both PanZ overexpression-linked β-alanine auxotrophy and pentyl pantothenamide toxicity are due to formation of this complex. This both demonstrates that the PanDZ complex regulates pantothenate biosynthesis in a cellular context and validates the complex as a target for antibiotic development. PubMed: 28832133DOI: 10.1021/acs.biochem.7b00509 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.16 Å) |
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