6NTE
Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)
6NTE の概要
| エントリーDOI | 10.2210/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 | |
| 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: 32786290DOI: 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) |
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