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KMID : 0545120230330040485
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Journal of Microbiology and Biotechnology
2023 Volume.33 No. 4 p.485 ~ p.492
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Crystal Structure of Mesaconyl-CoA Hydratase from Methylorubrum extorquens CM4
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Ahn Jae-Woo
Hong Ji-Yeon
Kim Kyung-Jin
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Abstract
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Methylorubrum extorquens, a facultative methylotroph, assimilates C1 compounds and accumulates poly-β-hydroxylbutyrate (PHB) as carbon and energy sources. The ethylmalonyl pathway is central to the carbon metabolism of M. extorquens, and is linked with a serine cycle and a PHB biosynthesis pathway. Understanding the ethylmalonyl pathway is vital in utilizing methylotrophs to produce value-added chemicals. In this study, we determined the crystal structure of the mesaconyl-CoA hydratase from M. extorquens (MeMeaC) that catalyzes the reversible conversion of mesaconyl-CoA to β-methylmalyl-CoA. The crystal structure of MeMeaC revealed that the enzyme belongs to the MaoC-like dehydratase domain superfamily and functions as a trimer. In our current MeMeaC structure, malic acid occupied the substrate binding site, which reveals how MeMeaC recognizes the β-methylmalyl-moiety of its substrate. The active site of the enzyme was further speculated by comparing its structure with those of other MaoC-like hydratases.
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KEYWORD
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Mesaconyl-CoA hydratase, Methylorubrum extorquens, ethylmalonyl pathway, crystal structure
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