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6NTE

Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)

6NTE の概要
エントリーDOI10.2210/pdb6nte/pdb
分子名称Dihydroxy-acid dehydratase (2 entities in total)
機能のキーワードdehydratase, lyase
由来する生物種Synechocystis sp. PCC 6803
タンパク質・核酸の鎖数2
化学式量合計117395.79
構造登録者
MacTavish, B.,Bruner, S. (登録日: 2019-01-29, 公開日: 2020-03-04, 最終更新日: 2024-10-30)
主引用文献Zhang, P.,MacTavish, B.S.,Yang, G.,Chen, M.,Roh, J.,Newsome, K.R.,Bruner, S.D.,Ding, Y.
Cyanobacterial Dihydroxyacid Dehydratases Are a Promising Growth Inhibition Target.
Acs Chem.Biol., 15:2281-2288, 2020
Cited by
PubMed Abstract: Microbes are essential to the global ecosystem, but undesirable microbial growth causes issues ranging from food spoilage and infectious diseases to harmful cyanobacterial blooms. The use of chemicals to control microbial growth has achieved significant success, while specific roles for a majority of essential genes in growth control remain unexplored. Here, we show the growth inhibition of cyanobacterial species by targeting an essential enzyme for the biosynthesis of branched-chain amino acids. Specifically, we report the biochemical, genetic, and structural characterization of dihydroxyacid dehydratase from the model cyanobacterium sp. PCC 6803 (SnDHAD). Our studies suggest that SnDHAD is an oxygen-stable enzyme containing a [2Fe-2S] cluster. Furthermore, we demonstrate that SnDHAD is selectively inhibited and by the natural product aspterric acid, which also inhibits the growth of representative bloom-forming and strains but has minimal effects on microbial pathogens with [4Fe-4S] containing DHADs. This study suggests DHADs as a promising target for the precise growth control of microbes and highlights the exploration of other untargeted essential genes for microbial management.
PubMed: 32786290
DOI: 10.1021/acschembio.0c00507
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.33 Å)
構造検証レポート
Validation report summary of 6nte
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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