8HLG

Crystal structure of MoaE

Summary for 8HLG

• Entry DOI: 10.2210/pdb8hlg/pdb
• Descriptor: Molybdenum cofactor biosynthesis protein D/E, SULFATE ION (3 entities in total)
• Functional Keywords: cofactor, biosynthesis, transferase
• Biological source: Deinococcus radiodurans R1
• Total number of polymer chains: 2
• Total formula weight: 38411.06

Authors

Cai, J.,Zhao, Y. (deposition date: 2022-11-30, release date: 2023-10-18, Last modification date: 2024-11-27)

Primary citation

Cai, J.,Zhang, M.,Chen, Z.,Zhao, Y.,Xu, H.,Tian, B.,Wang, L.,Hua, Y.
MoaE Is Involved in Response to Oxidative Stress in Deinococcus radiodurans.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: Molybdenum ions are covalently bound to molybdenum pterin (MPT) to produce molybdenum cofactor (Moco), a compound essential for the catalytic activity of molybdenum enzymes, which is involved in a variety of biological functions. MoaE is the large subunit of MPT synthase and plays a key role in Moco synthesis. Here, we investigated the function of MoaE in (DrMoaE) in vitro and in vivo, demonstrating that the protein contributed to the extreme resistance of . The crystal structure of DrMoaE was determined by 1.9 Å resolution. DrMoaE was shown to be a dimer and the dimerization disappeared after Arg110 had been mutated. The deletion of resulted in sensitivity to DNA damage stress and a slower growth rate in . The increase in transcript levels the and accumulation of intracellular reactive oxygen species levels under oxidative stress suggested that it was involved in the antioxidant process in . In addition, treatment with the base analog 6-hydroxyaminopurine decreased survival and increased intracellular mutation rates in deletion mutant strains. Our results reveal that MoaE plays a role in response to external stress mainly through oxidative stress resistance mechanisms in .

PubMed: 36768763
DOI: 10.3390/ijms24032441

Experimental method

X-RAY DIFFRACTION (2 Å)