6NTE

Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)

Summary for 6NTE

• Entry DOI: 10.2210/pdb6nte/pdb
• Descriptor: Dihydroxy-acid dehydratase (2 entities in total)
• Functional Keywords: dehydratase, lyase
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 2
• Total formula weight: 117395.79

Authors

MacTavish, B.,Bruner, S. (deposition date: 2019-01-29, release date: 2020-03-04, Last modification date: 2024-10-30)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2.33 Å)