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5LS7

Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ

5LS7 の概要
エントリーDOI10.2210/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
Monteiro, D.C.F.,Webb, M.E.,Pearson, A.R. (登録日: 2016-08-22, 公開日: 2017-09-13, 最終更新日: 2024-01-17)
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: 28832133
DOI: 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)
構造検証レポート
Validation report summary of 5ls7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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